-
127浏览
-
0点赞
-
0收藏
-
0分享
-
97下载
-
0评论
-
引用
期刊论文
A novel phospholipase A2/esterase from hyperthermophilic archaeon Aeropyrum pernix K1
Protein Expression and PuriWcation 35(2004)199-205,-0001,():
An open reading frame of the hyperthermophilic archaeon Aeropyrum pernix K1 APE2325, which composed of 474 bases, was cloned and expressed in Escherichia coli BL21 (DE3) Codon Plus-RIL. The recombinant protein was puriWed by Ni-chelation aYnity chromatography. It showed a single band with a molecular mass of 18kDa in SDS–PAGE. The puriWed enzyme exhibited both phospholipase A2 and esterase activities with the optimal catalytic temperature at 90℃. The enzyme activity was Ca2+-independent. Kinetic analysis revealed its Km, kcat, and Vm for the p-nitrophenyl propionate substrate were 103μM, 39s-1, and 249μmol/min/mg, respectively. The recombinant protein was thermostable and its half-life at 100℃ was about 1h.
【免责声明】以下全部内容由[冯雁]上传于[2011年02月18日 09时26分27秒],版权归原创者所有。本文仅代表作者本人观点,与本网站无关。本网站对文中陈述、观点判断保持中立,不对所包含内容的准确性、可靠性或完整性提供任何明示或暗示的保证。请读者仅作参考,并请自行承担全部责任。
本学者其他成果
同领域成果