Engineering of the [alpha]-amylase from Geobacillus stearothermophilus US100 for detergent incorporation

AmyUS100...IG is a variant of the most thermoactive and thermostable maltohexaose forming α- amylase produced by Geobacillus stearothermophilus sp.US100. This enzyme which was designed to improve the thermostability of the wild-type enzyme has acquired a very high resistance to chelator agents. Acco...

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Veröffentlicht in:Biotechnology and bioengineering 2009-02, Vol.102 (2), p.380-389
Hauptverfasser: Khemakhem, Bassem, Ali, Marndouh Ben, Aghajari, Nushin, Juy, Michel, Haser, Richard, Bejar, Samir
Format: Artikel
Sprache:eng
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Zusammenfassung:AmyUS100...IG is a variant of the most thermoactive and thermostable maltohexaose forming α- amylase produced by Geobacillus stearothermophilus sp.US100. This enzyme which was designed to improve the thermostability of the wild-type enzyme has acquired a very high resistance to chelator agents. According to modeling structural studies and with the aim of enhancing its resistance towards chemical oxidation, a mutant (AmyUS100...IG/M197A) was created by substituting methionine 197 to alanine. The catalytic proprieties of the resulting mutant show alterations in the specific activity and the profile of starch hydrolysis. Interestingly, AmyUS100...IG/M197A displayed the highest resistance to oxidation compared to the AmyUS100...IG and to Termamyl300..., the well-known commercial amylase used in detergent. Further, performance of the engineered α-amylase was estimated in the presence of commonly used detergent compounds and a wide range of commercial detergent (liquid and solid). These studies indicated a high compatibility and performance of AmyUS100...IG/M197A, suggesting its potential application in detergent industry. (ProQuest: ... denotes formulae/symbols omitted.)
ISSN:0006-3592
1097-0290
DOI:10.1002/bit.22083