Thermozymes: biotechnology and structure–function relationships
被引:1
作者:
J. G. Zeikus
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机构:Department of Biochemistry,
J. G. Zeikus
Claire Vieille
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h-index: 0
机构:Department of Biochemistry,
Claire Vieille
Alexei Savchenko
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h-index: 0
机构:Department of Biochemistry,
Alexei Savchenko
机构:
[1] Department of Biochemistry,
[2] Michigan State University,undefined
[3] 410 Biochemistry Building,undefined
[4] East Lansing,undefined
[5] MI 48824,undefined
[6] USA Tel. +1-517-336-4613; Fax +1-517-332-7810 e-mail: Zeikus@mbi.org,undefined
来源:
Extremophiles
|
1998年
/
2卷
关键词:
Key words Industrial enzymes;
Protein stability;
Thermophilicity;
D O I:
暂无
中图分类号:
学科分类号:
摘要:
Recent findings on the biochemical and molecular features of the following thermozymes are presented, based on their biotechnological use: α-amylase and amylopullulanase, used in starch processing; glucose isomerase, used in sweetener production; alcohol dehydrogenase, used in chemical synthesis; and alkaline phosphatase, used in diagnostics. The corresponding genes and recombinant proteins have been characterized in terms of sequence similarities, specific activities, thermophilicity, and unfolding kinetics. Site-directed and nested deletion mutagenesis were used to understand structure–function relationships. All these thermozymes display higher stability and activity than their counterparts currently used in the biotechnology industry.