Two detergent stable alkaline serine-proteases from Bacillus mojavensis A21: Purification, characterization and potential application as a laundry detergent additive

被引：233

作者：

Haddar, Anissa ^{[1
]}

Agrebi, Rym ^{[1
]}

Bougatef, Ali ^{[1
]}

Hmidet, Noomen ^{[1
]}

Sellami-Kamoun, Alya ^{[1
]}

Nasri, Moncef ^{[1
]}

机构：

[1] Ecole Nat Ingenieurs Sfax, Lab Genie Enzymat & Microbiol, Sfax 3038, Tunisia

来源：

BIORESOURCE TECHNOLOGY | 2009年 / 100卷 / 13期

关键词：

Alkaline proteases; Surfactant-stable; Detergent activity; Bacillus mojavensis; SUBTILISIN CARLSBERG; MOLECULAR-CLONING; GENE; LICHENIFORMIS; FORMULATIONS; PROTEINASES; EXPRESSION; STABILITY; TOLERANT; SALT;

D O I：

10.1016/j.biortech.2009.01.061

中图分类号：

S2 [农业工程];

学科分类号：

082806 [农业信息与电气工程];

摘要：

Two detergent stable alkaline serine-proteases (BM 1 and BM2) from Bacillus mojavensis A21 were purified. The molecular weights of BM1 and BM2 enzymes determined by SDS-PAGE were approximately 29.000 Da and 15,500 Da, respectively. The optimum pH values of BM 1 and BM2 proteases were shown to be 8.0-10.0 and 10.0. respectively. Both enzymes exhibited maximal activity at 60 degrees C, using casein as a substrate. The N-terminal amino acid sequences of BM1 and BM2 proteases were AQSVPYGISQIKA and AIPDQAATTLL, respectively. Both proteases showed high stability towards non-ionic surfactants. The enzymes were found to be relatively stable towards oxidizing agents. In addition, both enzymes showed excellent stability and compatibility with a wide range of commercial liquid and solid detergents. These properties and the high activity in high alkaline pH make these proteases an ideal choice for application in detergent formulations. (C) 2009 Elsevier Ltd. All rights reserved.

引用

页码：3366 / 3373

页数：8

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