Halophiles and their enzymes: negativity put to good use

被引:189
作者
DasSarma, Shiladitya [1 ]
DasSarma, Priya [1 ]
机构
[1] Univ Maryland, Inst Marine & Environm Technol, Dept Microbiol & Immunol, Sch Med,Columbus Ctr, Baltimore, MD 21202 USA
基金
美国国家卫生研究院;
关键词
PROTEIN; DEHYDROGENASE; ACTIVATION; STABILITY; CELLULASE;
D O I
10.1016/j.mib.2015.05.009
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Halophilic microorganisms possess stable enzymes that function in very high salinity, an extreme condition that leads to denaturation, aggregation, and precipitation of most other proteins. Genomic and structural analyses have established that the enzymes of halophilic Archaea and many halophilic Bacteria are negatively charged due to an excess of acidic over basic residues, and altered hydrophobicity, which enhance solubility and promote function in low water activity conditions. Here, we provide an update on recent bioinformatic analysis of predicted halophilic proteomes as well as experimental molecular studies on individual halophilic enzymes. Recent efforts on discovery and utilization of halophiles and their enzymes for biotechnology, including biofuel applications are also considered.
引用
收藏
页码:120 / 126
页数:7
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