Identification and characterization of a novel high-activity amylosucrase from Salinispirillum sp. LH10-3-1

被引：5

作者：

Li, Jing ^{[1
]}

Li, Ziyi ^{[1
]}

Gong, Hui ^{[1
]}

Ma, Mengyi ^{[1
]}

Li, Shuolei ^{[1
]}

Yang, Huilin ^{[1
]}

Zhang, Hailin ^{[1
]}

Liu, Jianguo ^{[1
]}

机构：

[1] China Univ Petr East China, Coll Chem & Chem Engn, Ctr Bioengn & Biotechnol, Qingdao 266580, Peoples R China

来源：

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY | 2023年 / 107卷 / 5-6期

基金：

中国国家自然科学基金;

关键词：

Amylosucrase; Salinispirillum sp; Expression; Characterization; alpha-Arbutin; GLUCAN-SYNTHESIZING ENZYME; RECOMBINANT AMYLOSUCRASE; FUNCTIONAL EXPRESSION; MOLECULAR-CLONING; ALPHA-ARBUTIN; OLIGOSACCHARIDE; BIOSYNTHESIS; HYDROQUINONE; PURIFICATION; GENE;

D O I：

10.1007/s00253-023-12430-6

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：

In this study, a novel high-activity amylosucrase from Salinispirillum sp. LH10-3-1 (SaAS) was identified and characterized. The recombinant enzyme was determined as a monomer with a molecular mass of 75 kDa. SaAS protein exhibited the maximum total and polymerization activities at pH 9.0 and maximum hydrolysis activity at pH 8.0. The optimum temperature for total, polymerization, and hydrolysis activities were 40, 40, and 45 & DEG;C, respectively. Under the optimal pH and temperature, SaAS had a specific activity of 108.2 U/mg. SaAS also showed excellent salt tolerance and could retain 77.4% of its original total activity at 4.0 M NaCl. The addition of Mg2+, Ba2+, and Ca2+ enhanced the total activity of SaAS. When the conversion of 0.1 M and 1.0 M sucrose was catalyzed at pH 9.0 and 40 ? for 24 h, the ratios of hydrolysis, polymerization, and isomerization reactions were 11.9:77.4:10.7 and 15.3:53.5:31.2, respectively. The alpha-arbutin yield of 60.3% was achieved from 20 mM sucrose and 5 mM hydroquinone catalyzed by SaAS.

引用

页码：1725 / 1736

页数：12

共 41 条

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