Nature Versus Nurture: Developing Enzymes That Function Under Extreme Conditions

被引:116
作者
Liszka, Michael J. [1 ]
Clark, Melinda E. [2 ]
Schneider, Elizabeth [1 ,3 ]
Clark, Douglas S. [1 ]
机构
[1] Univ Calif Berkeley, Dept Chem & Biomol Engn, Berkeley, CA 94720 USA
[2] Univ Calif Berkeley, Energy Biosci Inst, Berkeley, CA 94720 USA
[3] Univ Calif Berkeley, UC Berkeley & UCSF Grad Program Bioengn, Berkeley, CA 94720 USA
来源
ANNUAL REVIEW OF CHEMICAL AND BIOMOLECULAR ENGINEERING, VOL 3 | 2012年 / 3卷
关键词
protein engineering; bioprospecting; extremophiles; industrial biocatalysis; hydrolases; cellulases; ARCHAEON SULFOLOBUS-SOLFATARICUS; SOLVENT-STABLE PROTEASE; HIGH THERMAL-STABILITY; AMINO-ACID-RESIDUES; ANTARCTICA LIPASE-B; IONIC LIQUIDS; CRYSTAL-STRUCTURE; ALPHA-CHYMOTRYPSIN; BIOCHEMICAL-CHARACTERIZATION; DIRECTED EVOLUTION;
D O I
10.1146/annurev-chembioeng-061010-114239
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Many industrial processes used to produce chemicals and pharmaceuticals would benefit from enzymes that function under extreme conditions. Enzymes from extremophilic microorganisms have evolved to function in a variety of extreme environments, and bioprospecting for these microorganisms has led to the discovery of new enzymes with high tolerance to nonnatural conditions. However, bioprospecting is inherently limited by the diversity of enzymes evolved by nature. Protein engineering has also been successful in generating extremophilic enzymes by both rational mutagenesis and directed evolution, but screening for activity under extreme conditions can be difficult. This review examines the emerging synergy between bioprospecting and protein engineering in developing extremophilic enzymes. Specific topics include unnatural industrial conditions relevant to biocatalysis, biophysical properties of extremophilic enzymes, and industrially relevant extremophilic enzymes found either in nature or through protein engineering.
引用
收藏
页码:77 / 102
页数:26
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