Document Detail


Evaluation of various ions and compounds on nitrilase produced from Streptomyces sp.
MedLine Citation:
PMID:  20047516     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The nitrilase produced from a new isolate is evaluated for its activity in presence of a number of different ions and compounds at optimal conditions. It was found that the activity of nitrilase increased up to 10-20% in presence of most of the divalent ions at a concentration of 5 mM relative to the control. Silver, mercury, tin, DTT, ascorbic acid and thiourea, respectively, were observed as potential inhibitors of the enzyme catalysis. The investigation on storage stability of whole cells in presence of a number of stabilizers showed that the enzyme is stable (relative activity 50%) for more than 120 days at various temperatures.
Authors:
Amit Kumar Khandelwal; Vinod Kumar Nigam; Ambarish S Vidyarthi; Purnendu Ghosh
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Artificial cells, blood substitutes, and immobilization biotechnology     Volume:  38     ISSN:  1532-4184     ISO Abbreviation:  Artif Cells Blood Substit Immobil Biotechnol     Publication Date:  2010  
Date Detail:
Created Date:  2010-01-19     Completed Date:  2010-06-10     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9431307     Medline TA:  Artif Cells Blood Substit Immobil Biotechnol     Country:  England    
Other Details:
Languages:  eng     Pagination:  13-8     Citation Subset:  IM    
Affiliation:
Birla Institute of Scientific Research, Jaipur, Rajasthan, India.
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MeSH Terms
Descriptor/Qualifier:
Aminohydrolases / antagonists & inhibitors,  chemistry,  metabolism*
Biodegradation, Environmental
Cations, Divalent / chemistry,  metabolism*,  pharmacology
Industrial Microbiology
Metals / chemistry,  metabolism*,  pharmacology
Nitriles / metabolism*
Protein Stability / drug effects
Sanitary Engineering / methods
Streptomyces / enzymology*
Temperature
Chemical
Reg. No./Substance:
0/Cations, Divalent; 0/Metals; 0/Nitriles; EC 3.5.4.-/Aminohydrolases; EC 3.5.5.1/nitrilase

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