Document Detail


Stability of thermostable alkaline protease from Bacillus licheniformis RP1 in commercial solid laundry detergent formulations.
MedLine Citation:
PMID:  16872818     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The stability of crude extracellular protease produced by Bacillus licheniformis RP1, isolated from polluted water, in various solid laundry detergents was investigated. The enzyme had an optimum pH and temperature at pH 10.0-11.0 and 65-70 degrees C. Enzyme activity was inhibited by PMSF, suggesting that the preparation contains a serine-protease. The alkaline protease showed extreme stability towards non-ionic (5% Tween 20% and 5% Triton X-100) and anionic (0.5% SDS) surfactants, which retained 100% and above 73%, respectively, of its initial activity after preincubation 60 min at 40 degrees C. The RP1 protease showed excellent stability and compatibility with a wide range of commercial solid detergents at temperatures from 40 to 50 degrees C, suggesting its further application in detergent industry. The enzyme retained 95% of its initial activity with Ariel followed by Axion (94%) then Dixan (93.5%) after preincubation 60 min at 40 degrees C in the presence of 7 mg/ml of detergents. In the presence of Nadhif and New Det, the enzyme retained about 83.5% of the original activity. The effects of additives such as maltodextrin, sucrose and PEG 4000 on the stability of the enzyme during spray-drying and during subsequent storage in New Det detergent were also examined. All additives tested enhanced stability of the enzyme.
Authors:
Alya Sellami-Kamoun; Anissa Haddar; Nedra El-Hadj Ali; Basma Ghorbel-Frikha; Safia Kanoun; Moncef Nasri
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-07-26
Journal Detail:
Title:  Microbiological research     Volume:  163     ISSN:  0944-5013     ISO Abbreviation:  Microbiol. Res.     Publication Date:  2008  
Date Detail:
Created Date:  2008-04-14     Completed Date:  2008-07-03     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9437794     Medline TA:  Microbiol Res     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  299-306     Citation Subset:  IM    
Affiliation:
Laboratoire de Génie Enzymatique et de Microbiologie-Ecole Nationale d'Ingénieurs de Sfax, Sfax, Tunisia.
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MeSH Terms
Descriptor/Qualifier:
Bacillus / enzymology*,  isolation & purification
Bacterial Proteins / chemistry*,  metabolism*
Detergents / pharmacology*
Endopeptidases / chemistry*,  metabolism*
Enzyme Inhibitors / pharmacology*
Enzyme Stability
Hydrogen-Ion Concentration
Octoxynol / pharmacology
Phenylmethylsulfonyl Fluoride / pharmacology
Polysorbates / pharmacology
Sodium Dodecyl Sulfate / pharmacology
Temperature
Water Microbiology
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Detergents; 0/Enzyme Inhibitors; 0/Polysorbates; 151-21-3/Sodium Dodecyl Sulfate; 329-98-6/Phenylmethylsulfonyl Fluoride; 9002-93-1/Octoxynol; EC 3.4.-/Endopeptidases; EC 3.4.99.-/alkaline protease

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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