Enzymatic conversion of D-galactose to D-tagatose: Cloning, overexpression and characterization of L-arabinose isomerase from Pediococcus pentosaceus PC-5

被引：47
作者：
Men, Yan [1 ]
Zhu, Yueming [1 ]
Zhang, Lili [1 ]
Kang, Zhenkui [2 ]
Izumori, Ken [1 ]
Sun, Yuanxia [1 ]
Ma, Yanhe [1 ]
机构：
[1] Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Natl Engn Lab Ind Enzymes, Tianjin 300308, Peoples R China
[2] Shanxi Tianjiao Biol Co Ltd, Shanxin 030006, Peoples R China
来源：
MICROBIOLOGICAL RESEARCH | 2014年 / 169卷 / 2-3期
基金：
中国国家自然科学基金;
关键词：
L-Arabinose isomerase; D-Tagatose; Food-grade microorganisms; Pediococcus pentosaceus; THERMAL-STABILITY; GLUCOSE ISOMERASE; ESCHERICHIA-COLI; SWISS-MODEL; PURIFICATION; EXPRESSION; BIOCONVERSION;
D O I：
10.1016/j.micres.2013.07.001
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
The gene encoding L-arabinose isomerase from food-grade strain Pediococcus pentosaceus PC-5 was cloned and overexpressed in Escherichia coli. The recombinant protein was purified and characterized. It was optimally active at 50 degrees C and pH 6.0. Furthermore, this enzyme exhibited a weak requirement for metallic ions for its maximal activity evaluated at 0.6 mM Mn2+ or 0.8 mM Co2+. Interestingly, this enzyme was distinguished from other L-AIs, it could not use L-arabinose as its substrate. In addition, a three-dimensional structure of L.-AI was built by homology modeling and L-arabinose and D-galactose were docked into the active site pocket of PPAI model to explain the interaction between L-AI and its substrate. The purified P. pentosaceus PC-5 L-AI converted P-galactose into D-tagatose with a high conversion rate of 52% after 24 h at 50 degrees C, suggesting its excellent potential in D-tagatose production. Crown Copyright (C) 2013 Published by Elsevier GmbH. All rights reserved.
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页码：171 / 178
页数：8
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