Document Detail


Production and partial characterization of extracellular amylase enzyme from Bacillus amyloliquefaciens P-001.
MedLine Citation:
PMID:  23626928     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Amylases are one of the most important enzymes in present-day biotechnology. The present study was concerned with the production and partial characterization of extracellular amylase from Bacillus amyloliquefaciens P-001. The effect of various fermentation conditions on amylase production through shake-flask culture was investigated. Enzyme production was induced by a variety of starchy substrate but corn flour was found to be a suitable natural source for maximum production. Tryptone and ammonium nitrate (0.2%) as nitrogen sources gave higher yield compared to other nitrogen sources. Maximum enzyme production was obtained after 48 hrs of incubation in a fermentation medium with initial pH 9.0 at 42°C under continuous agitation at 150 rpm. The size of inoculum was also optimized which was found to be 1% (v/v). Enzyme production was 2.43 times higher after optimizing the production conditions as compared to the basal media. Studies on crude amylase revealed that optimum pH, temperature and reaction time of enzyme activity was 6.5, 60°C and 40 minutes respectively. About 73% of the activity retained after heating the crude enzyme solution at 50°C for 30 min. The enzyme was activated by Ca(2+) (relative activity 146.25%). It was strongly inhibited by Mn(2+), Zn(2+) and Cu(2+), but less affected by Mg(2+) and Fe(2+).
Authors:
Promita Deb; Saimon Ahmad Talukdar; Kaniz Mohsina; Palash Kumar Sarker; Sm Abu Sayem
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-4-10
Journal Detail:
Title:  SpringerPlus     Volume:  2     ISSN:  2193-1801     ISO Abbreviation:  Springerplus     Publication Date:  2013 Dec 
Date Detail:
Created Date:  2013-4-29     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101597967     Medline TA:  Springerplus     Country:  -    
Other Details:
Languages:  ENG     Pagination:  154     Citation Subset:  -    
Affiliation:
Department of Genetic Engineering and Biotechnology, Shahjalal University of Science and Technology, Sylhet, Bangladesh.
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