Characterization and stability studies on surfactant, detergent and oxidant stable α-amylase from marine haloalkaliphilic Saccharopolyspora sp. A9

被引:83
作者
Chakraborty, Samrat [2 ]
Khopade, Abhijeet [2 ]
Biao, Ren [3 ]
Jian, Wang [3 ]
Liu, Xiang-Yang [3 ]
Mahadik, Kakasaheb [2 ]
Chopade, Balasaheb [4 ]
Zhang, Lixin [3 ]
Kokare, Chandrakant [1 ,2 ]
机构
[1] STES Sinhgad Inst Pharm, Pune 411041, Maharashtra, India
[2] Bharati Vidyapeeth Univ, Poona Coll Pharm, Dept Pharmaceut Biotechnol, Pune 411038, Maharashtra, India
[3] Chinese Acad Sci, Key Lab Pathogen Microbiol & Immunol, Inst Microbiol, Beijing 100101, Peoples R China
[4] Univ Pune, Inst Bioinformat & Biotechnol, Pune 411007, Maharashtra, India
关键词
alpha-Amylase; Halophilic; Thermostable; Surfactant; Oxidant stable; BACILLUS SP; RAW STARCH; ENZYMATIC-PROPERTIES; ALKALINE PROTEASE; PURIFICATION; MICROORGANISMS; ISOLATE;
D O I
10.1016/j.molcatb.2010.09.009
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 halopalkaliphilic marine Saccharopolyspora sp stain A9 with an ability to produce surfactants oxidant and detergent stable a-amylase was Isolated from marine sediments collected from west coast of India The a-amylase from strain A9 was purified to homogeneity with the aid of ammonium sulfate precipitation and gel filtration chromatography by using Sephadex G-75 insoluble corn starch and sephacryl S-100 column with a 3901-fold increase in specific activity SDS-PAGE and zymogram activity staining showed a single band equal to molecular mass of 66 kDa Enzyme was found to be stable in presence of wide range of NaCl concentration with maximum activity found at 11% (w/v) of NaCl Enzyme showed remarkable stability towards laboratory surfactants detergents and oxidants Glucose maltose and maltotnose were the main end product of starch hydrolysis indicating it is a-amylase (c) 2010 Elsevier B V All rights reserved
引用
收藏
页码:52 / 58
页数:7
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