Can lipases hydrolyze a peptide bond?

被引：18

作者：

Maruyama, T

Nakajima, M

Kondo, H

Kawasaki, K

Seki, M

Goto, M

机构：

[1] Natl Food Res Inst, Tsukuba, Ibaraki 3058642, Japan

[2] Univ Tokyo, Grad Sch Engn, Dept Chem & Biotechnol, Bunkyo Ku, Tokyo 1138656, Japan

[3] Natl Inst Adv Ind Sci & Technol, AIST, Struct Biol Grp, Res Inst Biol Sci, Sapporo, Hokkaido 0628517, Japan

[4] Kyushu Univ, Grad Sch Engn, Dept Appl Chem, Fukuoka 8128581, Japan

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 2003年 / 32卷 / 06期

关键词：

hydrolysis; lipase; peptidase activity; serine protease; MISCIBLE ORGANIC-SOLVENTS; CATALYZED SYNTHESIS; AMINO-ACID; RESOLUTION; CUTINASE; ENZYME;

D O I：

10.1016/S0141-0229(03)00053-X

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

Several research groups reported that lipase catalyzes peptide synthesis in organic solvents. Structural studies revealed that the catalytic triad of lipase consists of Ser, His, and Asp, the same as serine proteases. Lipase has a potential to have peptidase activity. In this report, we investigated the peptidase activity of lipases. Of 13 lipases of diverse origin tested, only commercially available porcine pancreatic lipase (PPL) exhibited peptidase activity. However, purification of PPL by gel permeation chromatography separated the peptidase and lipolytic activities of PPL. This study clearly demonstrated that all the lipases tested do not hydrolyze a peptide bond. (C) 2003 Elsevier Science Inc. All rights reserved.

引用

页码：655 / 657

页数：3

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