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 |
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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.) |
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ISSN: | 0006-3592 1097-0290 |
DOI: | 10.1002/bit.22083 |