Production, purification and biochemical characterization of a novel detergent-stable serine alkaline protease from Bacillus safensis strain RH12

被引：70

作者：

Rekik, Hatem ^{[1
,2
,3
]}

Jaouadi, Nadia Zarai ^{[1
,2
]}

Gargouri, Fares ^{[1
]}

Bejar, Wacim ^{[1
]}

Frikha, Fakher ^{[1
]}

Jmal, Najah ^{[3
]}

Bejar, Samir ^{[1
,2
]}

Jaouadi, Bassem ^{[1
,2
]}

机构：

[1] Univ Sfax, CBS, LMBEE, Rd Sidi Mansour Km 6,POB 1177, Sfax 3018, Tunisia

[2] Univ Sfax, Biotech ECOZYM Start Up, Business Incubator, CBS, Rd Sidi Mansour Km 6,POB 1177, Sfax 3018, Tunisia

[3] STE JMAL EJM Laundry Detergent Ind, ZI Ave August 13,ZI Poudriere 1,POB 407, Boustene 3000, Sfax, Tunisia

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2019年 / 121卷

关键词：

Protease; Bacillus safensis; Offshore oil field; Detergent; Wash performance; MOLECULAR CHARACTERIZATION; PUMILUS CBS; LICHENIFORMIS STRAIN; KERATINASE; PROTEINASE; COMPATIBILITY; EXPRESSION; STABILITY; ENZYMES;

D O I：

10.1016/j.ijbiomac.2018.10.139

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：

A novel extracellular protease (SAPRH) was hyper-produced (9000 U/mL) from Bacillus safensis RH12, a newly isolated enzyme from a Tunisian offshore oil field. The enzyme was purified to homogeneity, using salt precipitation, heat-treatment and FPLC anion-exchange chromatography. The purified enzyme was a monomer of molecular mass of similar to 28 kDa. The NH2-terminal 23 amino-acid sequence of SAPRH showed high homology with those of Bacillus-proteases. SAPRH displayed optimal activity at pH 9 and 60 degrees C. It was strongly inhibited by phenylmethanesulfonyl fluoride (PMSF) and diiodopropyl fluorophosphates (DFP), indicating that it belongs to the serine-proteases family. Moreover, SAPRH was extremely stable at a broad range of temperature and pH retaining 85% of its activity at 50 degrees C and 75% at pH 11. The enzyme exhibited excellent stability and compatibility with surfactants and commercial detergents, revealing 90% stability with SDS and 100% stability with Class commercial laundry detergent. One of the most distinctive properties is its catalytic efficiency, which is higher than that of Alcalase 2.51, typeDX (commercial enzyme) and SAPB from B. pumilus CBS. Interestingly, the results of the wash performance analysis demonstrated considerably good de-staining at 40 degrees C for 30 min with low supplementation (500 U/mL). Accordingly, such a protease could be considered as a good detergent-additive in detergent industry. (C) 2018 Published by Elsevier B.V.

引用

页码：1227 / 1239

页数：13