Characterization of a family IV esterase from extremely halophilic archaeon Haloarcula japonica

被引：0
|
作者：
Kato, Hiromichi [1 ]
Ambai, Shota [1 ]
Ikeda, Fumiya [1 ]
Abe, Koji [1 ]
Nakamura, Satoshi [1 ]
Yatsunami, Rie [1 ]
机构：
[1] Inst Sci Tokyo, Sch Life Sci & Technol, 4259 Nagatsuta,Midori Ku, Yokohama 2268501, Japan
来源：
EXTREMOPHILES | 2025年 / 29卷 / 01期
关键词：
Esterase; Family IV; Hormone-sensitive lipase family; Halophilic esterase; Extremely halophilic archaeon; Haloarcula japonica; HORMONE-SENSITIVE LIPASE; CELL-SURFACE GLYCOPROTEIN; THERMOSTABLE ESTERASE; SUBSTRATE-SPECIFICITY; SEQUENCE SIMILARITY; SHUTTLE VECTORS; PROTEINS; CARBOXYLESTERASE; INSIGHTS; ENZYMES;
D O I：
10.1007/s00792-024-01370-2
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The novel esterase gene lipP1, which encodes HjEstP1, was discovered in the genome of the extremely halophilic archaeon Haloarcula japonica. A homology search and sequence alignment revealed that HjEstP1 is a member of family IV esterases with conserved GXSXG and HGGG motifs. lipP1 was expressed in its parental strain, and recombinant HjEstP1 was purified and characterized. Optimal pH and temperature of HjEstP1 were 6.0 and > 60 degrees C, respectively. HjEstP1 showed higher activity with increasing NaCl concentration, and optimal NaCl concentration was > 4.5 M. Furthermore, HjEstP1 preferentially hydrolyzed pNP and glycerol esters with short chain fatty acids. To our knowledge, this is the first report of an esterase from an extremely halophilic archaeon obtained via homologous expression.
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页数：9
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