dc.description.abstract |
Actinomycetes are a suitable microbial group for the synthesis of lignocellulose-degrading enzymes. Enzymes that may degrade organic material, including cellulose, hemicellulose, and lignin, are released by actinomycetes. The aim of this research was to isolate actinomycetes from Rajkot, Gujarat, India’s soil and evaluate the activity of their cellulase and Xylanase enzymes. Starch Casein Agar (SCA) was used to identify a total of 30 isolates of actinomycetes. A qualitative plate assay (CMC-Na, Congo red) revealed that the highest zone of catalysis for MMD1 was 36 mm. Five strains were discovered to be effective for quantitative quantification of endoglucanase utilising filter paper and CMC as substrates: MMD1, MMD2, MMD3, MMD4, and MMD8. Following MMD 1 (endoglucanase 5.4 IU; FPase 4.4 IU), MMD 2 (endoglucanase 4.5 IU; FPase 3.4 IU) has demonstrated considerable endoglucanase and FPase activity. Beechwood xylan was used to treat sugarcane bagasse in order to test Xylanase, and 45% of the xylan (hemicellulose) fraction was obtained. MMD1 and MMD2 measured the xylanase enzyme activity (4.8 IU and 4.2 IU) in quantitative and qualitative assays (34 mm and 22 mm for BWX and 32 mm and 14 mm for agro-waste xylan). The strain MMD1 was identified as Streptomyces chartreusis through morphological, biochemical, and finally molecular characterization by 16S rRNA sequencing. It was then submitted to NCBI GenBank with the accession number MT254830.
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