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嗜碱性芽孢杆菌碱性α淀粉酶的纯化和性质
引用本文:吴襟,彭平,沈文,马延和,张树政.嗜碱性芽孢杆菌碱性α淀粉酶的纯化和性质[J].中国生物化学与分子生物学报,2005,21(6):852-856.
作者姓名:吴襟  彭平  沈文  马延和  张树政
作者单位:1. 中国科学院微生物研究所,北京,100080
2. 中国科学院微生物研究所,北京,100080;新疆石河子大学动物科技学院,石河子,832003
基金项目:国家高科技研究发展计划项目(863)(No.2004AA214060),中国科学院知识创新工程重要方向项目(No.KSCX2SW323)~~
摘    要:淀粉是高等植物体内碳水化合物的主要储藏形式,广泛存在于谷物、豆类的种子和果实中.α1,4葡聚糖4葡聚糖水解酶(α1,4glucan4glucanohydrolase,EC3.2.1.1),又简称为α淀粉酶(αamylase),能水解淀粉分子内部α1,4葡萄糖苷键,水解产物有糊精、麦芽寡糖、麦芽糖和葡萄糖.它和β淀粉酶、α葡萄糖苷酶、去分枝酶(普鲁兰酶)和异淀粉酶等都属于糖苷水解酶13家族,即α淀粉酶家族1].α淀粉酶是目前世界上最早生产、产量最大的工业酶制剂品种之一,在食品、纺织、医药和饲料等工业中都有非常重要的应用;其中碱性α淀粉酶常用于洗涤剂和纺织品工业中,…

关 键 词:α-amylase  purification  and  characterization  alkaliphilic  Bacillus  sp.  
收稿时间:2005-12-20
修稿时间:2005年1月25日

Purification and Characterization of a-Amylase from an Alkaliphilic Bacillus sp.strain BG-CSN
WU Jin,PENG Ping,SHEN Wen,MA Yan-He,ZHANG Shu-Zheng.Purification and Characterization of a-Amylase from an Alkaliphilic Bacillus sp.strain BG-CSN[J].Chinese Journal of Biochemistry and Molecular Biology,2005,21(6):852-856.
Authors:WU Jin  PENG Ping  SHEN Wen  MA Yan-He  ZHANG Shu-Zheng
Institution:( 1)Institute of Microbiology,Chinese Academy of Sciences,Beijing 100080,China; 2)College of Animal Science and Technology,Shihezi University,Shihezi 832003,China
Abstract:One Gram-positive bacteria,Bacillus sp.strain BG-CSN,was isolated from the muds with hypersaline and alkaline water at the beach of Banger Soda Lake in Tibet,China.After cultivating in liquid medium for 48 hours,an extracellular α-amylase AmyBGC from the strain BG-CSN was purified 23-fold reaching to electrophoretic homogeneity by sequentially ammonium sulfate precipitation,Octyl-Sepharose CL-4B column chromatography,DEAE-Sepharose Fast Flow chromatography,DEAE-Toyopearl 650M chromatography and Sephadex G-100 chromatography.The enzyme had a molecular mass of 87 kD estimated by SDS-PAGE.The enzyme was optimally active at pH 10.5 and 52.5℃ and showed stability at pH range of 5.0 to 11.5 at the temperature below 35℃. The enzyme activity was inhibited by Hg+ and Fe 3+.The activity was not prevented at all by chelating reagents EDTA and SDS at high concentrations.This enzyme efficiently hydrolyzed starch to yield a series of maltooligosaccharides,including maltose after completion of the reaction.These results indicate that AmyBGC is classified as a liquefying endo-1,4-D-α-amylase(EC-3.2.1.1).
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