A novel phospholipase A2/esterase from hyperthermophilic archaeon Aeropyrum pernix K1

被引：19
|
作者：
Wang, BJ [1 ]
Lu, DM [1 ]
Gao, RJ [1 ]
Yang, Z [1 ]
Cao, SG [1 ]
Feng, Y [1 ]
机构：
[1] Jilin Univ, Key Lab Mol Enzymol & Engn, Minist Educ, Changchun 130023, Peoples R China
来源：
PROTEIN EXPRESSION AND PURIFICATION | 2004年 / 35卷 / 02期
关键词：
Aeropyrum pernix K-1; phospholipase A(2); esterase; thermostability;
D O I：
10.1016/j.pep.2004.01.010
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
An open reading frame of the hyperthermophilic archaeon Aeropyrum pernix K-1 APE2325, which composed of 474 bases, was cloned and expressed in Escherichia coli BL21 (DE3) Codon Plus-RIL. The recombinant protein was purified by Ni-chelation affinity chromatography. It showed a single band with a molecular mass of 18 kDa in SDS-PAGE. The purified enzyme exhibited both phospholipase A(2) and esterase activities with the optimal catalytic temperature at 90degreesC. The enzyme activity was Ca2+-independent. Kinetic analysis revealed its K-m, k(cat), and V-m for the p-nitrophenyl propionate substrate were 103 muM, 39 s(-1), and 249 mumol/min/mg, respectively. The recombinant protein was thermostable and its half-life at 100 degreesC was about I h. (C) 2004 Elsevier Inc. All rights reserved.
引用
收藏
页码：199 / 205
页数：7
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