Abstract:
L-asparaginase has its applications in medicine for the treatment of cancer and in food industry to mitigate the production of acrylamide in starchy foods. This research project aimed to isolate and characterize L-asparaginase producing bacteria. The bacteria were isolated (n = 7) from the oil contaminated soil, grown on M9 modified media to confirm the ability to metabolize L-asparagine and subjected to biochemical and molecular characterization. All the isolates showed positive results for casein, gelatin and starch hydrolysis, catalase production and citrate utilization test. While 05 strains (ASP2, ASP3, ASP4, ASP11 and ASP13) were positive for H2S production test. Quantitative enzymatic assays were performed to investigate the relative enzyme activity of bacterial L-asparaginases. Result revealed higher activity of L asparaginase in case of ASP2, ASP11, and ASP 20, while ASP3, ASP4, ASP12, ASP 13, and ASP30 were found least active. Molecular characterization of isolates was carried out through 16s rRNA profiling. The PCR amplified products of 16S rRNA gene were sent to Macrogen, Korea for Sanger sequencing. The sequences obtained were subjected to the BLAST analysis to check out the similarity with sequences available at NCBI. Sequences of the isolates were submitted to NCBI, and Accession No. were assigned to them. Isolated strains, ASP2 showed 95.39% similarity with Sarratia odoriferous strain DSM 4582, ASP3 was found to show 70.09% similarity with Raoultella ornithinolytica Strain JCM6096, ASP4 exhibited 93.33% similarity with Serratia rubidaea strain NBRC 103169, ASP11 showed 93.36% similarity with Pseudomonas straminea strain NBRC 16665, ASP13 was found similar to 93.53% similarity with Pseudomonas sagittaria strain CC-OPY-1, ASP20 exhibited 95.28% similarity with Enterobacter mori strain YIM Hb-3 and ASP30 strain showed 98.73% similarity with Acinetobacter junii strain Mannheim 2723/59 according to NCBI GenBank database. Results of the study are encouraging and thus propose future extension of search work for the isolation, purification of L-asparaginases for exploitation of commercial bases.
Page(s):
102-102
DOI:
DOI not available
Published:
Journal: Abstract Book on Global Science Technology and Management Conference, Volume: 0, Issue: 0, Year: 2023