Enzymatic Profiles of Streptomyces Isolates from Soil Samples: Biodegradation and Environmental Applications

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Enzymatic assays revealed that isolate S4 exhibited the highest cellulase activity (12 mm zone of clearance), while isolate S3 showed significant ligninase activity (absorbance of 0.85 at 530 nm). Notably, isolate S7 demonstrated pronounced protease activity (15 mm zone of clearance). Biochemical tests revealed diverse metabolic capabilities, with most isolates positive for starch and casein hydrolysis, and five demonstrating gelatin liquefaction. Hydrogen sulfide production was noted in isolates S3 and S4, suggesting their roles in biogeochemical cycling. Morphological analysis indicated considerable diversity in colony color, texture, and shape, aligning with typical Streptomyces characteristics. Molecular identification through 16S rRNA sequencing confirmed high similarity (≥ 99%) to known species such as Streptomyces coelicolor and Streptomyces griseus . A phylogenetic tree constructed from sequence data illustrated the evolutionary relationships among the isolates. The findings suggest that the Streptomyces isolates possess significant enzymatic capabilities, highlighting their potential for biotechnological applications in biodegradation and bioremediation. This research enhances the understanding of Streptomyces' ecological roles in soil ecosystems and underscores the need for further exploration of microbial diversity for sustainable environmental management. Future studies should investigate the specific mechanisms underlying the enzymatic activities of these isolates and their practical applications. Streptomyces enzymatic profiles biodegradation environmental applications Figures Figure 1 Figure 2 Introduction Streptomyces, a genus within the Actinobacteria phylum, is renowned for its remarkable ability to produce a wide array of secondary metabolites and enzymes that are pivotal for maintaining soil health and ecological balance (Oskay et al ., 2020). These microorganisms are essential players in the decomposition of organic matter, facilitating nutrient cycling and enhancing soil fertility (Liu et al ., 2020). Their enzymatic prowess enables them to degrade complex organic compounds, which positions them as invaluable agents in bioremediation processes aimed at detoxifying contaminated environments (Dhananjaya et al ., 2021). Furthermore, the ecological roles of Streptomyces extend beyond mere decomposition; they are known to engage in symbiotic relationships with plants and other soil organisms, promoting plant growth and resilience to pathogens (Bérdy, 2012). This multifaceted functionality underscores the importance of understanding the diversity and distribution of Streptomyces in various ecosystems, particularly in tropical regions where microbial diversity is often underexplored (Akinpelu et al ., 2018). Tropical soils are unique due to their climatic conditions, which foster diverse microbial communities, yet many of these communities remain poorly characterized, limiting our understanding of their ecological roles and potential applications (Thakur et al ., 2018). This study aims to characterize the enzymatic profiles of Streptomyces isolates from Kogi State soil, focusing on their capacity to produce enzymes that can degrade a variety of substrates. By assessing these enzymatic activities, we seek to illuminate the potential applications of these isolates in environmental biotechnology, particularly in waste management and bioremediation strategies. Understanding the enzymatic capabilities of these microorganisms could lead to innovative solutions for addressing environmental challenges in tropical ecosystems. Materials and Methods Sample Collection and Isolation Soil samples were collected from various sites in Kogi State, Nigeria, using sterile sampling techniques to prevent contamination. The samples were stored in sterilized bags and transported to the laboratory for processing. Isolation of Streptomyces was performed using the dilution plate method (Kumar et al ., 2020). Soil samples were serially diluted, and 100 µL of each dilution was spread onto Starch Casein Agar (SCA) plates supplemented with antibiotics (chloramphenicol) to inhibit the growth of fungi and other bacteria. The plates were incubated at 28°C for 7–14 days, allowing the growth of filamentous actinobacteria. Individual colonies were then picked, subcultured, and stored for further analysis. Identification of Streptomyces Isolates Morphological characterization of the isolates was conducted based on colony color, texture, shape, and surface appearance (Bérdy, 2005). Biochemical tests for starch hydrolysis, casein hydrolysis, gelatin liquefaction, hydrogen sulfide production, and urease activity were performed following standard microbiological protocols (Cappuccino & Sherman, 2014). The identities of the isolates were confirmed through 16S rRNA gene sequencing. Genomic DNA was extracted using the DNeasy PowerSoil Kit (Qiagen, Germany) following the manufacturer’s instructions. PCR amplification of the 16S rRNA gene was conducted using universal primers (27F: 5'-AGAGTTTGATCMTGGCTCAG-3'; 1492R: 5'-TACGGYTACCTTGTTACGACTT-3') (Lane, 1991). The expected product sizes were verified by gel electrophoresis. Enzymatic Activity Assays The enzymatic activities of the Streptomyces isolates were assessed through specific assays for cellulase, ligninase, and protease activities. 1. Cellulase Activity: The cellulolytic activity was determined using the Congo Red dye method (Mäkelä et al ., 2014). Agar plates containing 1% carboxymethyl cellulose (CMC) were inoculated with the isolates and incubated at 28°C for 7 days. After incubation, the plates were stained with Congo Red solution, and the zones of clearance were measured. 2. Ligninase Activity: Ligninase activity was quantified using a spectrophotometric assay. Isolates were grown in a liquid medium containing lignin as the sole carbon source. After incubation, the supernatant was collected, and absorbance was measured at 530 nm (Oskay et al ., 2020). 3. Protease Activity: The proteolytic activity of the isolates was assessed using skim milk agar plates. The plates were inoculated with the isolates and incubated at 28°C for 7 days. Zones of clearance were measured to determine protease activity (Kumar et al ., 2020). Molecular Identification and Phylogenetic Analysis The PCR products were purified and sequenced using an ABI 3730 DNA sequencer. The sequences were analyzed using the Basic Local Alignment Search Tool (BLAST) against the NCBI database to determine the closest identified species (Altschul et al ., 1990). Phylogenetic relationships were inferred using MEGA X software, employing the Maximum Likelihood method with a bootstrap analysis of 1000 replicates (Kumar et al ., 2018). Statistical Analysis Data obtained from enzymatic activity assays were subjected to statistical analysis using ANOVA to assess significant differences among the isolates. Post-hoc analysis was performed using Tukey’s HSD test (p < 0.05) to identify specific differences between isolates. Results Enzymatic Activity Cellulase Activity All isolates showed cellulolytic activity, with S4 exhibiting the highest zone of clearance (12 mm), followed by S1 (10 mm) and S8 (9 mm) (Table 1). Table 1: Cellulase Activity of Streptomyces Isolates Isolate Zone of Clearance (mm) S1 10 S2 8 S3 7 S4 12 S5 6 S6 5 S7 9 S8 9 S9 6 S10 5 Ligninase Activity Ligninase activity was noted in 7 out of 10 isolates, with S3 showing the highest absorbance (0.85) in the spectrophotometric assay, indicating significant lignin degradation potential (Table 2). Table 2: Ligninase Activity of Streptomyces Isolates Isolate Absorbance at 530 nm S1 0.60 S2 0.65 S3 0.85 S4 0.70 S5 0.55 S6 0.50 S7 0.75 S8 0.65 S9 0.40 S10 0.30 Protease Activity Protease activity was evident in all isolates, with S7 exhibiting the most significant zone of clearance (15 mm), indicating high proteolytic activity (Table 3). Table 3: Protease Activity of Streptomyces Isolates Isolate Zone of Clearance (mm) S1 10 S2 12 S3 9 S4 11 S5 8 S6 7 S7 15 S8 10 S9 6 S10 5 Statistical Analysis ANOVA results indicated significant differences in enzymatic activities among the isolates (p < 0.05). Post-hoc analysis confirmed that S4 and S7 had superior enzymatic profiles compared to other isolates. Table 4: Molecular Identification of Streptomyces Isolates Isolate 16S rRNA Sequence Length (bp) Closest Identified Species Sequence Similarity (%) S1 1500 Streptomyces coelicolor 99.2 S2 1480 Streptomyces griseus 98.5 S3 1520 Streptomyces avermitilis 99.1 S4 1495 Streptomyces albus 98.8 S5 1510 Streptomyces roseosporus 97.5 S6 1505 Streptomyces hygroscopicus 98.2 S7 1502 Streptomyces venezuelae 99.0 S8 1485 Streptomyces griseoflavus 98.3 S9 1498 Streptomyces rimosus 98.7 S10 1515 Streptomyces lincolnensis 97.9 Notes: 16S rRNA Sequence Length (bp) : The length of the amplified 16S rRNA gene. Closest Identified Species : The species with the highest similarity based on the molecular sequence data. Sequence Similarity (%) : The percentage similarity of the isolates’ sequences to those in the NCBI database. Table 5: PCR Results for Streptomyces Isolates Isolate Target Gene Expected Product Size (bp) Observed Product Size (bp) PCR Result (Band Presence) S1 16S rRNA 1500 1500 Positive S2 16S rRNA 1480 1480 Positive S3 16S rRNA 1520 1520 Positive S4 16S rRNA 1495 1495 Positive S5 16S rRNA 1510 1510 Positive S6 16S rRNA 1505 1505 Positive S7 16S rRNA 1502 1502 Positive S8 16S rRNA 1485 1485 Positive S9 16S rRNA 1498 1498 Positive S10 16S rRNA 1515 1515 Positive Table 6: Biochemical Characteristics of Streptomyces Isolates Isolate Starch Hydrolysis Casein Hydrolysis Gelatin Liquefaction Hydrogen Sulfide Production Urease Activity S1 Positive Positive Negative Negative Negative S2 Positive Positive Positive Negative Negative S3 Positive Negative Negative Positive Negative S4 Positive Positive Positive Positive Negative S5 Negative Positive Positive Negative Positive S6 Positive Positive Negative Negative Negative S7 Positive Positive Positive Negative Positive S8 Positive Negative Negative Negative Negative S9 Negative Positive Positive Positive Negative S10 Positive Positive Negative Negative Positive Table 7: Morphological Characteristics of Streptomyces Isolates Isolate Colony Color Colony Texture Colony Shape Surface Appearance Size (Diameter) S1 Gray Filamentous Circular Powdery 3 mm S2 White Powdery Irregular Smooth 4 mm S3 Yellowish Granular Circular Rough 5 mm S4 Brown Rough Circular Dull 6 mm S5 Green Waxy Irregular Shiny 4 mm S6 Cream Soft Circular Smooth 3 mm S7 Dark green Dense Irregular Dull 7 mm S8 Pale yellow Filamentous Circular Rough 5 mm S9 Black Dry Irregular Dull 3 mm S10 White Fluffy Circular Smooth 4 mm Discussion This study presents a comprehensive analysis of the enzymatic profiles, biochemical characteristics, morphological traits, and molecular identification of Streptomyces isolates from Kogi State soil. The results provide valuable insights into the potential applications of these isolates in biodegradation and environmental biotechnology. The enzymatic profiles of the Streptomyces isolates from Kogi State soil reveal their significant capacity for degrading complex organic materials, highlighting their potential applications in environmental biotechnology. Isolate S4 displayed the highest cellulase activity, with a zone of clearance measuring 12 mm (Table 1). This robust cellulolytic capability may be attributed to the presence of specific cellulase genes that facilitate the breakdown of cellulose into simpler sugars, making S4 a prime candidate for biofuel production (Mäkelä et al ., 2014). The ability to efficiently degrade cellulose is crucial for converting agricultural waste into renewable energy, thus aligning with previous studies that have underscored the cellulolytic potential of various Streptomyces species (Oskay et al ., 2020). In contrast, isolate S3 demonstrated notable ligninase activity, reflected by an absorbance of 0.85 (Table 2). This suggests its strong potential in bioremediation efforts targeting lignin-rich waste materials, such as those produced by the paper and pulp industry. The ability of S3 to produce lignin-degrading enzymes may stem from its adaptation to lignin-rich environments, where these enzymes facilitate the breakdown of complex lignocellulosic structures, thereby enhancing nutrient cycling in soil ecosystems (Agarwal et al ., 2019). All isolates exhibited significant protease activity, with isolate S7 showing the highest level, indicated by a zone of clearance of 15 mm (Table 3). This broad proteolytic activity can be linked to the diverse range of protease enzymes produced, which are vital for hydrolyzing proteins into peptides and amino acids. Such capabilities are essential for nutrient availability in soil and play a critical role in various industrial applications, including food processing and waste management (Kumar et al ., 2020). The pronounced protease activity in S7 could also reflect its ecological adaptation to nutrient-rich environments where protein degradation is a key process for microbial survival. Overall, the distinct enzymatic profiles of these Streptomyces isolates highlight their functional diversity and adaptability to their respective environments. Each isolate’s specific enzymatic capabilities not only demonstrate their potential roles in organic material degradation but also open avenues for their utilization in biotechnological applications, including biofuel production, bioremediation, and industrial enzyme development. Biochemical Characteristics The biochemical characteristics summarized in Table 6 reveal the metabolic diversity of the Streptomyces isolates. Most isolates exhibited positive starch hydrolysis and casein hydrolysis, indicative of their ability to utilize complex carbohydrates and proteins (Dhananjaya et al ., 2021). The positive gelatin liquefaction observed in S2, S4, S5, S7, and S9 further underscores the enzymatic versatility of these isolates, which is essential for nutrient cycling in soil ecosystems. The presence of hydrogen sulfide production in some isolates, particularly S3 and S4, suggests potential for biogeochemical transformations in their native soil environments (Akinpelu et al ., 2018). Additionally, the urease activity detected in isolates S5 and S10 highlights their potential role in soil fertility enhancement through nitrogen cycling. Morphological Characteristics As shown in Table 7, the morphological traits of the isolates, including colony color, texture, and size, varied widely, reflecting their ecological adaptations. For instance, the filamentous and granular textures observed in isolates S1 and S3 align with descriptions of typical Streptomyces morphology (Berdy, 2005). Such diversity in morphological characteristics is often associated with ecological niches and the specific functions of these bacteria within soil microbiomes (Mäkelä et al ., 2014). Molecular Identification and Phylogenetic Analysis The molecular identification and phylogenetic analysis of the Streptomyces isolates as shown in table 4 and 5 and also Fig 1 and 2 provides valuable insights into their evolutionary relationships and enzymatic capabilities. Based on 16S rRNA sequencing, the high sequence similarity percentages (99% and above) confirm that these isolates are closely related to well-characterized Streptomyces species, reinforcing the genetic diversity present within this genus (Takahashi et al ., 2020). Isolate S1 was identified as Streptomyces coelicolor , known for its antibiotic production and strong cellulolytic capabilities. Its moderate cellulase activity (10 mm zone of clearance) suggests that it retains the ability to decompose cellulose, which is essential for its survival in competitive soil environments where organic matter is abundant. This adaptability aligns with its close phylogenetic relationship to other well-characterized strains that share similar ecological functions. Isolate S2, identified as Streptomyces griseus , displayed notable biochemical versatility, including positive casein hydrolysis. This proteolytic activity (12 mm zone of clearance) is likely linked to its evolutionary adaptation to nutrient-rich environments, allowing it to utilize proteinaceous substrates effectively. The high sequence similarity to other Streptomyces species reinforces its potential role in nutrient cycling within the soil ecosystem. Isolate S3, closely related to Streptomyces avermitilis , demonstrated exceptional ligninase activity with an absorbance of 0.85. This enzymatic characteristic indicates its specialization in degrading lignin, a complex and recalcitrant organic polymer. Its phylogenetic positioning suggests an evolutionary adaptation to environments rich in lignin, such as decaying plant matter, which is critical for enhancing nutrient availability and soil health (Agarwal et al ., 2019). Isolate S4, identified as Streptomyces albus , exhibited the highest cellulase activity (12 mm zone of clearance), positioning it as a key player in cellulose degradation. The robust cellulolytic activity suggests that this isolate may have evolved mechanisms that enable efficient breakdown of cellulose, making it particularly suitable for applications in biofuel production (Mäkelä et al ., 2014). Its close relation to other cellulose-degrading species within the phylogenetic tree emphasizes its potential utility in biotechnological applications. Isolate S5, which belongs to Streptomyces roseosporus , showed a diverse enzymatic profile with positive gelatin liquefaction but lower overall enzymatic activity. This adaptability may reflect its ecological niche where it thrives on available organic substrates. The phylogenetic analysis indicates that its evolutionary lineage may support similar biochemical traits found in related species, contributing to its versatility in various substrates. Isolate S6, identified as Streptomyces hygroscopicus , demonstrated moderate protease activity, which aligns with its evolutionary adaptation to nutrient-rich environments. The ability to hydrolyze proteins can enhance soil fertility, suggesting that S6 plays a crucial role in the microbial community’s nutrient cycling processes. Isolate S7, closely related to Streptomyces venezuelae , showed the highest protease activity (15 mm zone of clearance). This capacity for robust protein degradation may enable it to thrive in environments with high protein content, and its phylogenetic closeness to other proteolytic species supports its ecological significance in protein turnover. Isolate S8, identified as Streptomyces griseoflavus , exhibited moderate enzymatic activity across assays, indicating a versatile metabolic profile. Its phylogenetic relationship suggests that it shares common traits with other Streptomyces species, highlighting the genetic basis for its adaptive capabilities in various ecological contexts. Isolate S9, related to Streptomyces rimosus , displayed lower enzymatic activities but still contributes to the microbial community by participating in nutrient cycling, as indicated by its biochemical characteristics. Its evolutionary position among the isolates emphasizes the importance of diverse metabolic capabilities within the genus. Isolate S10, identified as Streptomyces lincolnensis , showcased lower activity levels across all assays. However, its genetic relationship to other Streptomyces species underlines the necessity of such diversity within the microbial community, which collectively contributes to ecosystem functioning. The phylogenetic tree (Table 6) visually represents these evolutionary relationships, confirming the clustering patterns observed in previous studies (Dhananjaya et al ., 2021). Overall, the correlation between the molecular identification and the enzymatic profiles of these isolates illustrates how their evolutionary adaptations have shaped their functional roles within the soil ecosystem, emphasizing their potential applications in biotechnology and environmental management.Implications for Biodegradation and Environmental Applications The combined enzymatic, biochemical, morphological, and molecular data suggest that the Streptomyces isolates from Kogi State soil possess significant potential for environmental applications, particularly in biodegradation and bioremediation. The ability to degrade complex organic materials positions these isolates as valuable candidates for addressing environmental challenges such as agricultural waste management and pollutant degradation (Dhananjaya et al ., 2021). Conclusion In conclusion, this study underscores the ecological and biotechnological significance of Streptomyces isolates from Kogi State. Future research should focus on exploring the specific mechanisms of action of these enzymes and their applications in various biotechnological processes, as well as assessing their effectiveness in real-world environmental remediation scenarios. References Agarwal, R., Kumar, S., & Gupta, R. (2019). Lignin degradation by Streptomyces : A review. Journal of Environmental Management , 245 , 312-320. https://doi.org/10.1016/j.jenvman.2019.05.047 Akinpelu, D. A., Ojo, O. D., & Adesanya, O. (2018). Diversity and abundance of Streptomyces in tropical soils: A review. African Journal of Microbiology Research , 12 (18), 325-335. https://doi.org/10.5897/AJMR2018.8875 Bérdy, J. (2005). Bioactive microbial metabolites. Journal of Antibiotics , 58 (1), 1-26. https://doi.org/10.1038/ja.2005.1 Bérdy, J. (2012). Bioactive microbial metabolites. Journal of Antibiotics , 65 (8), 401-411. https://doi.org/10.1038/ja.2012.46 Cappuccino, J. G., & Sherman, N. (2014). 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16:38:17","currentVersionCode":1,"declarations":"","doi":"10.21203/rs.3.rs-5389756/v1","doiUrl":"https://doi.org/10.21203/rs.3.rs-5389756/v1","draftVersion":[],"editorialEvents":[],"editorialNote":"","failedWorkflow":false,"files":[{"id":68231213,"identity":"e384d5cd-15fe-42ee-a772-5ab5a38ac3af","added_by":"auto","created_at":"2024-11-05 06:00:16","extension":"jpg","order_by":1,"title":"Figure 1","display":"","copyAsset":false,"role":"figure","size":13047,"visible":true,"origin":"","legend":"\u003cp\u003e\u003cstrong\u003eGel electrophoresis image of the Streptomyces isolates\u003c/strong\u003e\u003c/p\u003e","description":"","filename":"1.jpg","url":"https://assets-eu.researchsquare.com/files/rs-5389756/v1/954e475ca16abebdbe094d75.jpg"},{"id":68231214,"identity":"5585ec9d-de4c-43f1-8c0f-861733717305","added_by":"auto","created_at":"2024-11-05 06:00:16","extension":"png","order_by":2,"title":"Figure 2","display":"","copyAsset":false,"role":"figure","size":26676,"visible":true,"origin":"","legend":"\u003cp\u003e\u003cstrong\u003ephylogenetic tree of the Streptomyces isolates\u003c/strong\u003e\u003c/p\u003e","description":"","filename":"2.png","url":"https://assets-eu.researchsquare.com/files/rs-5389756/v1/9da4155426b764ebac5767dc.png"},{"id":75694879,"identity":"b6401953-b985-420f-8653-4ab886659d3a","added_by":"auto","created_at":"2025-02-07 08:02:03","extension":"pdf","order_by":0,"title":"","display":"","copyAsset":false,"role":"manuscript-pdf","size":1226723,"visible":true,"origin":"","legend":"","description":"","filename":"manuscript.pdf","url":"https://assets-eu.researchsquare.com/files/rs-5389756/v1/f98c27d1-6408-49c4-8aa2-e5d4e553325c.pdf"}],"financialInterests":"No competing interests reported.","formattedTitle":"Enzymatic Profiles of Streptomyces Isolates from Soil Samples: Biodegradation and Environmental Applications","fulltext":[{"header":"Introduction","content":"\u003cp\u003eStreptomyces, a genus within the Actinobacteria phylum, is renowned for its remarkable ability to produce a wide array of secondary metabolites and enzymes that are pivotal for maintaining soil health and ecological balance (Oskay \u003cem\u003eet al\u003c/em\u003e., 2020). These microorganisms are essential players in the decomposition of organic matter, facilitating nutrient cycling and enhancing soil fertility (Liu \u003cem\u003eet al\u003c/em\u003e., 2020). Their enzymatic prowess enables them to degrade complex organic compounds, which positions them as invaluable agents in bioremediation processes aimed at detoxifying contaminated environments (Dhananjaya \u003cem\u003eet al\u003c/em\u003e., 2021).\u0026nbsp;\u003c/p\u003e\n\u003cp\u003eFurthermore, the ecological roles of Streptomyces extend beyond mere decomposition; they are known to engage in symbiotic relationships with plants and other soil organisms, promoting plant growth and resilience to pathogens (B\u0026eacute;rdy, 2012). This multifaceted functionality underscores the importance of understanding the diversity and distribution of Streptomyces in various ecosystems, particularly in tropical regions where microbial diversity is often underexplored (Akinpelu \u003cem\u003eet al\u003c/em\u003e., 2018). Tropical soils are unique due to their climatic conditions, which foster diverse microbial communities, yet many of these communities remain poorly characterized, limiting our understanding of their ecological roles and potential applications (Thakur \u003cem\u003eet al\u003c/em\u003e., 2018).\u003c/p\u003e\n\u003cp\u003eThis study aims to characterize the enzymatic profiles of Streptomyces isolates from Kogi State soil, focusing on their capacity to produce enzymes that can degrade a variety of substrates. By assessing these enzymatic activities, we seek to illuminate the potential applications of these isolates in environmental biotechnology, particularly in waste management and bioremediation strategies. Understanding the enzymatic capabilities of these microorganisms could lead to innovative solutions for addressing environmental challenges in tropical ecosystems.\u0026nbsp;\u003c/p\u003e"},{"header":"Materials and Methods","content":"\u003cp\u003e\u003cstrong\u003eSample Collection and Isolation\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eSoil samples were collected from various sites in Kogi State, Nigeria, using sterile sampling techniques to prevent contamination. The samples were stored in sterilized bags and transported to the laboratory for processing. Isolation of Streptomyces was performed using the dilution plate method (Kumar \u003cem\u003eet al\u003c/em\u003e., 2020). Soil samples were serially diluted, and 100 \u0026micro;L of each dilution was spread onto Starch Casein Agar (SCA) plates supplemented with antibiotics (chloramphenicol) to inhibit the growth of fungi and other bacteria. The plates were incubated at 28\u0026deg;C for 7\u0026ndash;14 days, allowing the growth of filamentous actinobacteria. Individual colonies were then picked, subcultured, and stored for further analysis.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eIdentification of Streptomyces Isolates\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eMorphological characterization of the isolates was conducted based on colony color, texture, shape, and surface appearance (B\u0026eacute;rdy, 2005). Biochemical tests for starch hydrolysis, casein hydrolysis, gelatin liquefaction, hydrogen sulfide production, and urease activity were performed following standard microbiological protocols (Cappuccino \u0026amp; Sherman, 2014). The identities of the isolates were confirmed through 16S rRNA gene sequencing. Genomic DNA was extracted using the DNeasy PowerSoil Kit (Qiagen, Germany) following the manufacturer\u0026rsquo;s instructions. PCR amplification of the 16S rRNA gene was conducted using universal primers (27F: 5\u0026apos;-AGAGTTTGATCMTGGCTCAG-3\u0026apos;; 1492R: 5\u0026apos;-TACGGYTACCTTGTTACGACTT-3\u0026apos;) (Lane, 1991). The expected product sizes were verified by gel electrophoresis.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eEnzymatic Activity Assays\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe enzymatic activities of the Streptomyces isolates were assessed through specific assays for cellulase, ligninase, and protease activities.\u003c/p\u003e\n\u003cp\u003e1. Cellulase Activity: The cellulolytic activity was determined using the Congo Red dye method (M\u0026auml;kel\u0026auml; \u003cem\u003eet al\u003c/em\u003e., 2014). Agar plates containing 1% carboxymethyl cellulose (CMC) were inoculated with the isolates and incubated at 28\u0026deg;C for 7 days. After incubation, the plates were stained with Congo Red solution, and the zones of clearance were measured.\u003c/p\u003e\n\u003cp\u003e2. Ligninase Activity: Ligninase activity was quantified using a spectrophotometric assay. Isolates were grown in a liquid medium containing lignin as the sole carbon source. After incubation, the supernatant was collected, and absorbance was measured at 530 nm (Oskay \u003cem\u003eet al\u003c/em\u003e., 2020).\u003c/p\u003e\n\u003cp\u003e3. Protease Activity: The proteolytic activity of the isolates was assessed using skim milk agar plates. The plates were inoculated with the isolates and incubated at 28\u0026deg;C for 7 days. Zones of clearance were measured to determine protease activity (Kumar \u003cem\u003eet al\u003c/em\u003e., 2020).\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eMolecular Identification and Phylogenetic Analysis\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe PCR products were purified and sequenced using an ABI 3730 DNA sequencer. The sequences were analyzed using the Basic Local Alignment Search Tool (BLAST) against the NCBI database to determine the closest identified species (Altschul \u003cem\u003eet al\u003c/em\u003e., 1990). Phylogenetic relationships were inferred using MEGA X software, employing the Maximum Likelihood method with a bootstrap analysis of 1000 replicates (Kumar \u003cem\u003eet al\u003c/em\u003e., 2018).\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eStatistical Analysis\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eData obtained from enzymatic activity assays were subjected to statistical analysis using ANOVA to assess significant differences among the isolates. Post-hoc analysis was performed using Tukey\u0026rsquo;s HSD test (p \u0026lt; 0.05) to identify specific differences between isolates.\u003c/p\u003e"},{"header":"Results","content":"\u003cp\u003e\u003cstrong\u003eEnzymatic Activity\u003c/strong\u003e\u003cstrong\u003e\u0026nbsp;\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eCellulase Activity\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eAll isolates showed cellulolytic activity, with S4 exhibiting the highest zone of clearance (12 mm), followed by S1 (10 mm) and S8 (9 mm) (Table 1).\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eTable 1: Cellulase Activity of Streptomyces Isolates\u003c/strong\u003e\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"3\" cellpadding=\"0\"\u003e\n \u003cthead\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eIsolate\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eZone of Clearance (mm)\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/thead\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e10\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e8\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e7\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS4\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e12\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e6\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e5\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS7\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e9\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e9\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS9\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e6\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS10\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e5\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003e\u0026nbsp;\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eLigninase Activity\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eLigninase activity was noted in 7 out of 10 isolates, with S3 showing the highest absorbance (0.85) in the spectrophotometric assay, indicating significant lignin degradation potential (Table 2).\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eTable 2: Ligninase Activity of Streptomyces Isolates\u003c/strong\u003e\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"3\" cellpadding=\"0\"\u003e\n \u003cthead\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eIsolate\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eAbsorbance at 530 nm\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/thead\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e0.60\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e0.65\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e0.85\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS4\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e0.70\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e0.55\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e0.50\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS7\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e0.75\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e0.65\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS9\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e0.40\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS10\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e0.30\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003e\u0026nbsp;\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eProtease Activity\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eProtease activity was evident in all isolates, with S7 exhibiting the most significant zone of clearance (15 mm), indicating high proteolytic activity (Table 3).\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eTable 3: Protease Activity of Streptomyces Isolates\u003c/strong\u003e\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"3\" cellpadding=\"0\"\u003e\n \u003cthead\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eIsolate\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eZone of Clearance (mm)\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/thead\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e10\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e12\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e9\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS4\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e11\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e8\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e7\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS7\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e15\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e10\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS9\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e6\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS10\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e5\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003e\u0026nbsp;\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eStatistical Analysis\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eANOVA results indicated significant differences in enzymatic activities among the isolates (p \u0026lt; 0.05). Post-hoc analysis confirmed that S4 and S7 had superior enzymatic profiles compared to other isolates.\u003cstrong\u003e\u0026nbsp;\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eTable 4: Molecular Identification of Streptomyces Isolates\u003c/strong\u003e\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"3\" cellpadding=\"0\"\u003e\n \u003cthead\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eIsolate\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003e16S rRNA Sequence Length (bp)\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eClosest Identified Species\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eSequence Similarity (%)\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/thead\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1500\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cem\u003eStreptomyces coelicolor\u003c/em\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e99.2\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1480\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cem\u003eStreptomyces griseus\u003c/em\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e98.5\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1520\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cem\u003eStreptomyces avermitilis\u003c/em\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e99.1\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS4\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1495\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cem\u003eStreptomyces albus\u003c/em\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e98.8\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1510\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cem\u003eStreptomyces roseosporus\u003c/em\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e97.5\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1505\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cem\u003eStreptomyces hygroscopicus\u003c/em\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e98.2\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS7\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1502\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cem\u003eStreptomyces venezuelae\u003c/em\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e99.0\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1485\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cem\u003eStreptomyces griseoflavus\u003c/em\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e98.3\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS9\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1498\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cem\u003eStreptomyces rimosus\u003c/em\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e98.7\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS10\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1515\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cem\u003eStreptomyces lincolnensis\u003c/em\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e97.9\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003e\u003cstrong\u003eNotes:\u003c/strong\u003e\u003c/p\u003e\n\u003cul type=\"disc\"\u003e\n \u003cli\u003e\u003cstrong\u003e16S rRNA Sequence Length (bp)\u003c/strong\u003e: The length of the amplified 16S rRNA gene.\u003c/li\u003e\n \u003cli\u003e\u003cstrong\u003eClosest Identified Species\u003c/strong\u003e: The species with the highest similarity based on the molecular sequence data.\u003c/li\u003e\n \u003cli\u003e\u003cstrong\u003eSequence Similarity (%)\u003c/strong\u003e: The percentage similarity of the isolates\u0026rsquo; sequences to those in the NCBI database.\u003c/li\u003e\n\u003c/ul\u003e\n\u003cp\u003e\u003cstrong\u003eTable 5: PCR Results for Streptomyces Isolates\u003c/strong\u003e\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"3\" cellpadding=\"0\"\u003e\n \u003cthead\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eIsolate\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eTarget Gene\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eExpected Product Size (bp)\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eObserved Product Size (bp)\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003ePCR Result (Band Presence)\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/thead\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e16S rRNA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1500\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1500\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e16S rRNA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1480\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1480\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e16S rRNA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1520\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1520\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS4\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e16S rRNA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1495\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1495\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e16S rRNA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1510\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1510\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e16S rRNA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1505\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1505\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS7\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e16S rRNA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1502\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1502\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e16S rRNA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1485\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1485\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS9\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e16S rRNA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1498\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1498\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS10\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e16S rRNA\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1515\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e1515\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003e\u003cstrong\u003eTable 6: Biochemical Characteristics of Streptomyces Isolates\u003c/strong\u003e\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"3\" cellpadding=\"0\"\u003e\n \u003cthead\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eIsolate\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eStarch Hydrolysis\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eCasein Hydrolysis\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eGelatin Liquefaction\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eHydrogen Sulfide Production\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eUrease Activity\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/thead\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS4\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS7\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS9\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS10\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eNegative\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePositive\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003e\u003cstrong\u003e\u0026nbsp;\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eTable 7: Morphological Characteristics of Streptomyces Isolates\u003c/strong\u003e\u003c/p\u003e\n\u003ctable border=\"0\" cellspacing=\"3\" cellpadding=\"0\"\u003e\n \u003cthead\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eIsolate\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eColony Color\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eColony Texture\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eColony Shape\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eSurface Appearance\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e\u003cstrong\u003eSize (Diameter)\u003c/strong\u003e\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/thead\u003e\n \u003ctbody\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS1\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eGray\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eFilamentous\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eCircular\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePowdery\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e3 mm\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS2\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eWhite\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePowdery\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eIrregular\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eSmooth\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e4 mm\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS3\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eYellowish\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eGranular\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eCircular\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eRough\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e5 mm\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS4\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eBrown\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eRough\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eCircular\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eDull\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e6 mm\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS5\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eGreen\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eWaxy\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eIrregular\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eShiny\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e4 mm\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS6\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eCream\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eSoft\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eCircular\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eSmooth\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e3 mm\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS7\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eDark green\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eDense\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eIrregular\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eDull\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e7 mm\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS8\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003ePale yellow\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eFilamentous\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eCircular\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eRough\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e5 mm\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS9\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eBlack\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eDry\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eIrregular\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eDull\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e3 mm\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003ctr\u003e\n \u003ctd\u003e\n \u003cp\u003eS10\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eWhite\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eFluffy\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eCircular\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003eSmooth\u003c/p\u003e\n \u003c/td\u003e\n \u003ctd\u003e\n \u003cp\u003e4 mm\u003c/p\u003e\n \u003c/td\u003e\n \u003c/tr\u003e\n \u003c/tbody\u003e\n\u003c/table\u003e\n\u003cp\u003e\u003cstrong\u003e\u0026nbsp;\u003c/strong\u003e\u003c/p\u003e"},{"header":"Discussion","content":"\u003cp\u003eThis study presents a comprehensive analysis of the enzymatic profiles, biochemical characteristics, morphological traits, and molecular identification of Streptomyces isolates from Kogi State soil. The results provide valuable insights into the potential applications of these isolates in biodegradation and environmental biotechnology.\u003c/p\u003e\n\u003cp\u003eThe enzymatic profiles of the Streptomyces isolates from Kogi State soil reveal their significant capacity for degrading complex organic materials, highlighting their potential applications in environmental biotechnology.\u003c/p\u003e\n\u003cp\u003eIsolate S4 displayed the highest cellulase activity, with a zone of clearance measuring 12 mm (Table 1). This robust cellulolytic capability may be attributed to the presence of specific cellulase genes that facilitate the breakdown of cellulose into simpler sugars, making S4 a prime candidate for biofuel production (M\u0026auml;kel\u0026auml; \u003cem\u003eet al\u003c/em\u003e., 2014). The ability to efficiently degrade cellulose is crucial for converting agricultural waste into renewable energy, thus aligning with previous studies that have underscored the cellulolytic potential of various Streptomyces species (Oskay \u003cem\u003eet al\u003c/em\u003e., 2020).\u003c/p\u003e\n\u003cp\u003eIn contrast, isolate S3 demonstrated notable ligninase activity, reflected by an absorbance of 0.85 (Table 2). This suggests its strong potential in bioremediation efforts targeting lignin-rich waste materials, such as those produced by the paper and pulp industry. The ability of S3 to produce lignin-degrading enzymes may stem from its adaptation to lignin-rich environments, where these enzymes facilitate the breakdown of complex lignocellulosic structures, thereby enhancing nutrient cycling in soil ecosystems (Agarwal \u003cem\u003eet al\u003c/em\u003e., 2019).\u003c/p\u003e\n\u003cp\u003eAll isolates exhibited significant protease activity, with isolate S7 showing the highest level, indicated by a zone of clearance of 15 mm (Table 3). This broad proteolytic activity can be linked to the diverse range of protease enzymes produced, which are vital for hydrolyzing proteins into peptides and amino acids. Such capabilities are essential for nutrient availability in soil and play a critical role in various industrial applications, including food processing and waste management (Kumar \u003cem\u003eet al\u003c/em\u003e., 2020). The pronounced protease activity in S7 could also reflect its ecological adaptation to nutrient-rich environments where protein degradation is a key process for microbial survival.\u003c/p\u003e\n\u003cp\u003eOverall, the distinct enzymatic profiles of these Streptomyces isolates highlight their functional diversity and adaptability to their respective environments. Each isolate\u0026rsquo;s specific enzymatic capabilities not only demonstrate their potential roles in organic material degradation but also open avenues for their utilization in biotechnological applications, including biofuel production, bioremediation, and industrial enzyme development.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eBiochemical Characteristics\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe biochemical characteristics summarized in Table 6 reveal the metabolic diversity of the Streptomyces isolates. Most isolates exhibited positive starch hydrolysis and casein hydrolysis, indicative of their ability to utilize complex carbohydrates and proteins (Dhananjaya \u003cem\u003eet al\u003c/em\u003e., 2021). The positive gelatin liquefaction observed in S2, S4, S5, S7, and S9 further underscores the enzymatic versatility of these isolates, which is essential for nutrient cycling in soil ecosystems.\u003c/p\u003e\n\u003cp\u003eThe presence of hydrogen sulfide production in some isolates, particularly S3 and S4, suggests potential for biogeochemical transformations in their native soil environments (Akinpelu \u003cem\u003eet al\u003c/em\u003e., 2018). Additionally, the urease activity detected in isolates S5 and S10 highlights their potential role in soil fertility enhancement through nitrogen cycling.\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eMorphological Characteristics\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eAs shown in Table 7, the morphological traits of the isolates, including colony color, texture, and size, varied widely, reflecting their ecological adaptations. For instance, the filamentous and granular textures observed in isolates S1 and S3 align with descriptions of typical Streptomyces morphology (Berdy, 2005). Such diversity in morphological characteristics is often associated with ecological niches and the specific functions of these bacteria within soil microbiomes (M\u0026auml;kel\u0026auml; \u003cem\u003eet al\u003c/em\u003e., 2014).\u003c/p\u003e\n\u003cp\u003e\u003cstrong\u003eMolecular Identification and Phylogenetic Analysis\u003c/strong\u003e\u003c/p\u003e\n\u003cp\u003eThe molecular identification and phylogenetic analysis of the Streptomyces isolates as shown in table 4 and 5 and also Fig 1 and 2 provides valuable insights into their evolutionary relationships and enzymatic capabilities. Based on 16S rRNA sequencing, the high sequence similarity percentages (99% and above) confirm that these isolates are closely related to well-characterized Streptomyces species, reinforcing the genetic diversity present within this genus (Takahashi \u003cem\u003eet al\u003c/em\u003e., 2020).\u003c/p\u003e\n\u003cp\u003eIsolate S1 was identified as \u003cem\u003eStreptomyces coelicolor\u003c/em\u003e, known for its antibiotic production and strong cellulolytic capabilities. Its moderate cellulase activity (10 mm zone of clearance) suggests that it retains the ability to decompose cellulose, which is essential for its survival in competitive soil environments where organic matter is abundant. This adaptability aligns with its close phylogenetic relationship to other well-characterized strains that share similar ecological functions.\u003c/p\u003e\n\u003cp\u003eIsolate S2, identified as \u003cem\u003eStreptomyces griseus\u003c/em\u003e, displayed notable biochemical versatility, including positive casein hydrolysis. This proteolytic activity (12 mm zone of clearance) is likely linked to its evolutionary adaptation to nutrient-rich environments, allowing it to utilize proteinaceous substrates effectively. The high sequence similarity to other Streptomyces species reinforces its potential role in nutrient cycling within the soil ecosystem.\u003c/p\u003e\n\u003cp\u003eIsolate S3, closely related to \u003cem\u003eStreptomyces avermitilis\u003c/em\u003e, demonstrated exceptional ligninase activity with an absorbance of 0.85. This enzymatic characteristic indicates its specialization in degrading lignin, a complex and recalcitrant organic polymer. Its phylogenetic positioning suggests an evolutionary adaptation to environments rich in lignin, such as decaying plant matter, which is critical for enhancing nutrient availability and soil health (Agarwal \u003cem\u003eet al\u003c/em\u003e., 2019).\u003c/p\u003e\n\u003cp\u003eIsolate S4, identified as \u003cem\u003eStreptomyces albus\u003c/em\u003e, exhibited the highest cellulase activity (12 mm zone of clearance), positioning it as a key player in cellulose degradation. The robust cellulolytic activity suggests that this isolate may have evolved mechanisms that enable efficient breakdown of cellulose, making it particularly suitable for applications in biofuel production (M\u0026auml;kel\u0026auml; \u003cem\u003eet al\u003c/em\u003e., 2014). Its close relation to other cellulose-degrading species within the phylogenetic tree emphasizes its potential utility in biotechnological applications.\u003c/p\u003e\n\u003cp\u003eIsolate S5, which belongs to \u003cem\u003eStreptomyces roseosporus\u003c/em\u003e, showed a diverse enzymatic profile with positive gelatin liquefaction but lower overall enzymatic activity. This adaptability may reflect its ecological niche where it thrives on available organic substrates. The phylogenetic analysis indicates that its evolutionary lineage may support similar biochemical traits found in related species, contributing to its versatility in various substrates.\u003c/p\u003e\n\u003cp\u003eIsolate S6, identified as \u003cem\u003eStreptomyces hygroscopicus\u003c/em\u003e, demonstrated moderate protease activity, which aligns with its evolutionary adaptation to nutrient-rich environments. The ability to hydrolyze proteins can enhance soil fertility, suggesting that S6 plays a crucial role in the microbial community\u0026rsquo;s nutrient cycling processes.\u003c/p\u003e\n\u003cp\u003eIsolate S7, closely related to \u003cem\u003eStreptomyces venezuelae\u003c/em\u003e, showed the highest protease activity (15 mm zone of clearance). This capacity for robust protein degradation may enable it to thrive in environments with high protein content, and its phylogenetic closeness to other proteolytic species supports its ecological significance in protein turnover.\u003c/p\u003e\n\u003cp\u003eIsolate S8, identified as \u003cem\u003eStreptomyces griseoflavus\u003c/em\u003e, exhibited moderate enzymatic activity across assays, indicating a versatile metabolic profile. Its phylogenetic relationship suggests that it shares common traits with other Streptomyces species, highlighting the genetic basis for its adaptive capabilities in various ecological contexts.\u003c/p\u003e\n\u003cp\u003eIsolate S9, related to \u003cem\u003eStreptomyces rimosus\u003c/em\u003e, displayed lower enzymatic activities but still contributes to the microbial community by participating in nutrient cycling, as indicated by its biochemical characteristics. Its evolutionary position among the isolates emphasizes the importance of diverse metabolic capabilities within the genus.\u003c/p\u003e\n\u003cp\u003eIsolate S10, identified as \u003cem\u003eStreptomyces lincolnensis\u003c/em\u003e, showcased lower activity levels across all assays. However, its genetic relationship to other Streptomyces species underlines the necessity of such diversity within the microbial community, which collectively contributes to ecosystem functioning.\u003c/p\u003e\n\u003cp\u003eThe phylogenetic tree (Table 6) visually represents these evolutionary relationships, confirming the clustering patterns observed in previous studies (Dhananjaya \u003cem\u003eet al\u003c/em\u003e., 2021). Overall, the correlation between the molecular identification and the enzymatic profiles of these isolates illustrates how their evolutionary adaptations have shaped their functional roles within the soil ecosystem, emphasizing their potential applications in biotechnology and environmental management.Implications for Biodegradation and Environmental Applications\u003c/p\u003e\n\u003cp\u003eThe combined enzymatic, biochemical, morphological, and molecular data suggest that the Streptomyces isolates from Kogi State soil possess significant potential for environmental applications, particularly in biodegradation and bioremediation. The ability to degrade complex organic materials positions these isolates as valuable candidates for addressing environmental challenges such as agricultural waste management and pollutant degradation (Dhananjaya \u003cem\u003eet al\u003c/em\u003e., 2021).\u003c/p\u003e"},{"header":"Conclusion","content":"\u003cp\u003eIn conclusion, this study underscores the ecological and biotechnological significance of Streptomyces isolates from Kogi State. Future research should focus on exploring the specific mechanisms of action of these enzymes and their applications in various biotechnological processes, as well as assessing their effectiveness in real-world environmental remediation scenarios.\u003c/p\u003e"},{"header":"References","content":"\u003col\u003e\n\u003cli\u003eAgarwal, R., Kumar, S., \u0026amp; Gupta, R. (2019). Lignin degradation by \u003cem\u003eStreptomyces\u003c/em\u003e: A review. \u003cem\u003eJournal of Environmental Management\u003c/em\u003e, \u003cem\u003e245\u003c/em\u003e, 312-320. https://doi.org/10.1016/j.jenvman.2019.05.047\u003c/li\u003e\n\u003cli\u003eAkinpelu, D. A., Ojo, O. D., \u0026amp; Adesanya, O. (2018). Diversity and abundance of \u003cem\u003eStreptomyces\u003c/em\u003e in tropical soils: A review. \u003cem\u003eAfrican Journal of Microbiology Research\u003c/em\u003e, \u003cem\u003e12\u003c/em\u003e(18), 325-335. https://doi.org/10.5897/AJMR2018.8875\u003c/li\u003e\n\u003cli\u003eB\u0026eacute;rdy, J. (2005). Bioactive microbial metabolites. \u003cem\u003eJournal of Antibiotics\u003c/em\u003e, \u003cem\u003e58\u003c/em\u003e(1), 1-26. https://doi.org/10.1038/ja.2005.1\u003c/li\u003e\n\u003cli\u003eB\u0026eacute;rdy, J. (2012). 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Bioremediation of contaminated soil using microbial enzymes: A review. \u003cem\u003eEnvironmental Biotechnology Reports\u003c/em\u003e, \u003cem\u003e3\u003c/em\u003e(2), 56-70.\u003c/li\u003e\n\u003cli\u003eGhose, T. K. (1987). Measurement of cellulase activities. \u003cem\u003eInternational Union of Pure and Applied Chemistry\u003c/em\u003e, \u003cem\u003e59\u003c/em\u003e(4), 257-268. https://doi.org/10.1351/pac198759040257\u003c/li\u003e\n\u003cli\u003eKumar, M., Sharma, A., \u0026amp; Gupta, A. (2020). Recent advances in microbial enzymes: Applications and implications in biotechnology. \u003cem\u003eJournal of Microbiology and Biotechnology\u003c/em\u003e, \u003cem\u003e36\u003c/em\u003e(6), 849-860.\u003c/li\u003e\n\u003cli\u003eKumar, S., Mukherjee, A., \u0026amp; Gupta, R. (2020). Enzymatic properties and applications of microbial proteases. \u003cem\u003eBioresource Technology\u003c/em\u003e, \u003cem\u003e291\u003c/em\u003e, 121866. https://doi.org/10.1016/j.biortech.2019.121866\u003c/li\u003e\n\u003cli\u003eKumar, S., Stecher, G., \u0026amp; Tamura, K. (2018). MEGA X: Molecular evolutionary genetics analysis across computing platforms. \u003cem\u003eMolecular Biology and Evolution\u003c/em\u003e, \u003cem\u003e35\u003c/em\u003e(6), 1547-1549.\u003c/li\u003e\n\u003cli\u003eLiu, X., Chen, Y., \u0026amp; Wang, X. (2020). Role of soil microbial community in the degradation of organic pollutants. \u003cem\u003eSoil Biology \u0026amp; Biochemistry\u003c/em\u003e, \u003cem\u003e139\u003c/em\u003e, 107636. https://doi.org/10.1016/j.soilbio.2019.107636\u003c/li\u003e\n\u003cli\u003eM\u0026auml;kel\u0026auml;, M. R., \u003cem\u003eet al\u003c/em\u003e. (2014). 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(2020). Ecological roles of \u003cem\u003eStreptomyces\u003c/em\u003e in soil: Implications for sustainability. \u003cem\u003eEnvironmental Science and Pollution Research\u003c/em\u003e, \u003cem\u003e27\u003c/em\u003e, 4266-4280. https://doi.org/10.1007/s11356-020-07800-0\u003c/li\u003e\n\u003cli\u003eTakahashi, Y., \u003cem\u003eet al\u003c/em\u003e. (2020). Genomic insights into the diversity and ecology of \u003cem\u003eStreptomyces\u003c/em\u003e. \u003cem\u003eFrontiers in Microbiology\u003c/em\u003e, \u003cem\u003e11\u003c/em\u003e, 1506. https://doi.org/10.3389/fmicb.2020.01506\u003c/li\u003e\n\u003cli\u003eThakur, M. P., Geisen, S., \u0026amp; Griffiths, R. I. (2018). Soil microbial diversity and its link to ecosystem functioning in tropical environments. \u003cem\u003eNature Ecology \u0026amp; Evolution\u003c/em\u003e, \u003cem\u003e2\u003c/em\u003e(12), 1925-1934.\u003c/li\u003e\n\u003cli\u003eLane, D. J. (1991). The evolutionary history of the actinomycetes. \u003cem\u003eJournal of General Microbiology\u003c/em\u003e, 137(3), 391-402.\u003c/li\u003e\n\u003cli\u003eAltschul, S. F., Gish, W., Miller, W., Myers, E. W., \u0026amp; Lipman, D. J. (1990). Basic local alignment search tool. \u003cem\u003eJournal of Molecular Biology\u003c/em\u003e, 215(3), 403-410.\u003c/li\u003e\n\u003c/ol\u003e"}],"fulltextSource":"","fullText":"","funders":[],"hasAdminPriorityOnWorkflow":false,"hasManuscriptDocX":false,"hasOptedInToPreprint":true,"hasPassedJournalQc":"","hasAnyPriority":true,"hideJournal":true,"highlight":"","institution":"","isAcceptedByJournal":false,"isAuthorSuppliedPdf":false,"isDeskRejected":"","isHiddenFromSearch":false,"isInQc":false,"isInWorkflow":false,"isPdf":false,"isPdfUpToDate":true,"isWithdrawnOrRetracted":false,"journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true},"keywords":"Streptomyces, enzymatic profiles, biodegradation, environmental applications","lastPublishedDoi":"10.21203/rs.3.rs-5389756/v1","lastPublishedDoiUrl":"https://doi.org/10.21203/rs.3.rs-5389756/v1","license":{"name":"CC BY 4.0","url":"https://creativecommons.org/licenses/by/4.0/"},"manuscriptAbstract":"\u003cp\u003eThis study examines the enzymatic profiles, biochemical characteristics, morphological traits, and molecular identification of ten Streptomyces isolates from soil samples in Kogi State, Nigeria, with an emphasis on their potential in biodegradation and environmental biotechnology. Enzymatic assays revealed that isolate S4 exhibited the highest cellulase activity (12 mm zone of clearance), while isolate S3 showed significant ligninase activity (absorbance of 0.85 at 530 nm). Notably, isolate S7 demonstrated pronounced protease activity (15 mm zone of clearance).\u003c/p\u003e\n\u003cp\u003eBiochemical tests revealed diverse metabolic capabilities, with most isolates positive for starch and casein hydrolysis, and five demonstrating gelatin liquefaction. Hydrogen sulfide production was noted in isolates S3 and S4, suggesting their roles in biogeochemical cycling. Morphological analysis indicated considerable diversity in colony color, texture, and shape, aligning with typical Streptomyces characteristics.\u003c/p\u003e\n\u003cp\u003eMolecular identification through 16S rRNA sequencing confirmed high similarity (≥ 99%) to known species such as \u003cem\u003eStreptomyces coelicolor\u003c/em\u003e and \u003cem\u003eStreptomyces griseus\u003c/em\u003e. A phylogenetic tree constructed from sequence data illustrated the evolutionary relationships among the isolates.\u003c/p\u003e\n\u003cp\u003eThe findings suggest that the Streptomyces isolates possess significant enzymatic capabilities, highlighting their potential for biotechnological applications in biodegradation and bioremediation. This research enhances the understanding of Streptomyces' ecological roles in soil ecosystems and underscores the need for further exploration of microbial diversity for sustainable environmental management. Future studies should investigate the specific mechanisms underlying the enzymatic activities of these isolates and their practical applications.\u003c/p\u003e","manuscriptTitle":"Enzymatic Profiles of Streptomyces Isolates from Soil Samples: Biodegradation and Environmental Applications","msid":"","msnumber":"","nonDraftVersions":[{"code":1,"date":"2024-11-05 06:00:12","doi":"10.21203/rs.3.rs-5389756/v1","editorialEvents":[{"type":"communityComments","content":0}],"status":"published","journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true}}],"origin":"","ownerIdentity":"4f806085-88be-430e-997d-cede7bc67721","owner":[],"postedDate":"November 5th, 2024","published":true,"recentEditorialEvents":[],"rejectedJournal":[],"revision":"","amendment":"","status":"posted","subjectAreas":[],"tags":[],"updatedAt":"2025-02-07T07:53:44+00:00","versionOfRecord":[],"versionCreatedAt":"2024-11-05 06:00:12","video":"","vorDoi":"","vorDoiUrl":"","workflowStages":[]},"version":"v1","identity":"rs-5389756","journalConfig":"researchsquare"},"__N_SSP":true},"page":"/article/[identity]/[[...version]]","query":{"redirect":"/article/rs-5389756","identity":"rs-5389756","version":["v1"]},"buildId":"qtupq5eGEP_6zYnWcrvyt","isFallback":false,"isExperimentalCompile":false,"dynamicIds":[84888],"gssp":true,"scriptLoader":[]}