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- W2158958137 endingPage "4056" @default.
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- W2158958137 abstract "Current theories agree that there appears to be no unique feature responsible for the remarkable heat stability properties of hyperthermostable proteins. A concerted action of structural, dynamic and other physicochemical attributes are utilized to ensure the delicate balance between stability and functionality of proteins at high temperatures. We have thoroughly screened the literature for hyperthermostable enzymes with optimal temperatures exceeding 100 degrees C that can potentially be employed in multiple biotechnological and industrial applications and to substitute traditionally used, high-cost engineered mesophilic/thermophilic enzymes that operate at lower temperatures. Furthermore, we discuss general methods of enzyme immobilization and suggest specific strategies to improve thermal stability, activity and durability of hyperthermophilic enzymes." @default.
- W2158958137 created "2016-06-24" @default.
- W2158958137 creator A5010586842 @default.
- W2158958137 creator A5016741183 @default.
- W2158958137 creator A5090226722 @default.
- W2158958137 date "2007-08-01" @default.
- W2158958137 modified "2023-10-17" @default.
- W2158958137 title "Hyperthermophilic enzymes − stability, activity and implementation strategies for high temperature applications" @default.
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