Enzymatic Properties of a Thermostable α-Glucosidase from Acidothermophilic Crenarchaeon Sulfolobus tokodaii Strain 7

被引：20

作者：

Park, Jung-Eun ^{[1
]}

Park, So Rae ^{[1
]}

Woo, Jung Yoon ^{[1
]}

Hwang, Hye Sun ^{[1
]}

Cha, Jaeho ^{[2
]}

Lee, Heeseob ^{[1
]}

机构：

[1] Pusan Natl Univ, Dept Food Sci & Nutr, Coll Human Ecol, Pusan 609735, South Korea

[2] Pusan Natl Univ, Dept Microbiol, Coll Nat Sci, Pusan 609735, South Korea

来源：

JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY | 2013年 / 23卷 / 01期

关键词：

Sulfolobus tokodaii strain 7; alpha-glucosidase; thermostability; transglycosylation; BIOCHEMICAL-CHARACTERIZATION; MALTOGENIC AMYLASE; PURIFICATION; GENE; ENZYMES; CLONING; IDENTIFICATION; TREHALOSE; SEQUENCE; MALTASE;

D O I：

10.4014/jmb.1210.10019

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

We have characterized the putative a-glucosidase gene (st2525) selected by total genome analysis from the acidothermophilic crenarchaeon Sulfolobus tokodaii strain 7. The ORE was cloned and expressed as a fusion protein in Escherichia coli, and recombinant ST2525 was purified by Ni-NTA affinity chromatography. Maximum activity was observed at 95 degrees C and pH 4.0, and the enzyme exhibited stability with half-lives of 40.1 min and 7.75 min at extremely high temperatures of 100 degrees C and 105 degrees C, respectively. The enzyme retained at least 85% of its maximal activity in the pH range of 4.0-11.0. ST2525 exclusively hydrolyzed alpha-1,4-glycosidic linkages of oligosaccharides in an exo-type manner, with highest catalytic efficiency toward maltotriose. The enzyme also displayed transglycosylation activity, converting maltose to isomaltose, panose, maltotriose, isomaltotriose, etc. From these results, ST2525 could be potentially useful for starch hydrolysis as well as novel synthesis of oligosaccharides in industry.

引用

页码：56 / 63

页数：8

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