Purification, physico-chemical characterization and sequence of a heat labile alkaline metalloprotease isolated from a psychrophilic Pseudomonas species

被引：38

作者：

Chessa, JP

Petrescu, I

Bentahir, M

Van Beeumen, J

Gerday, C

机构：

[1] Univ Liege, Biochem Lab, B-4000 Liege, Belgium

[2] Univ Ghent, Lab Biochem & Prot Engn, B-9000 Ghent, Belgium

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2000年 / 1479卷 / 1-2期

关键词：

psychrophile; alkaline metalloprotease; cold adaptation; Antarctic; immobilized metal affinity chromatography;

D O I：

10.1016/S0167-4838(00)00018-2

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 psychrophilic alkaline metalloprotease (PAP) produced by a Pseudomonas bacterium isolated from Antarctica has been purified and characterized. The gene encoding PAP has been cloned and sequenced and the derived amino acid sequence shows 66% identity with the mesophilic alkaline metalloprotease from Pseudomonas aeruginosa IFO 3455 (AP). Compared to the purified AP, PAP is three times more active at 20 degrees C, is very sensitive to chelating agents and is rapidly inactivated at 45 degrees C. The lower thermostability of PAP can tentatively be explained by a loss of a stabilizing Ca2+, a decrease in the content of hydrophobic residues and a smaller aliphatic index. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：265 / 274

页数：10

共 31 条

[1] Crystal structures of the psychrophilic α-amylase from Alteromonas haloplanctis in its native form and complexed with an inhibitor [J].