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Screening, Molecular characterization and assessment of profound protease activity from streptomyces glomeroauranticus vitsdvm6
, P.M. Lalitha, P.B. Shruthi, S. Jemimah Naine,
Published in Sphinx Knowledge House
2014
Volume: 6
   
Issue: 8
Pages: 4027 - 4032
Abstract
In the present study, actinomycetes were isolated from soil samples collected from the plant nursery at VIT University; eight different strains were isolated and screened for proteolytic property. The isolate exhibited profuse hydrolytic activity on casein media were considered as potent strain and was subjected to 16srDNA analysis. The BLAST search revealed the highest similarity with Streptomyces glomeroaurantiacus strain NBRC 15418, further the study strain was coined as Streptomyces glomeroaurantiacus VITSDVM6. The total protein contents of the crude enzyme extract, precipitated, dialysed and purified enzyme were determined by Lowry’s method. The specific activity was determined by casein hydrolysis assay which was found to have for the crude enzyme (897U/mg), Precipitated (1082 U/mg), dialysed (1285 U/mg) and purified (1336 U/mg) respectively. Hence the results showcase the productivity of Streptomyces glomeroaurantiacus VITSDVM6 as efficient producer of extra cellular protease, which can be beneficial for industries applications. © 2014, Sphinx Knowledge House. All rights reserved.
About the journal
JournalInternational Journal of ChemTech Research
PublisherSphinx Knowledge House
ISSN09744290
Open AccessNo