Enzymatic conversion of D-galactose to D-tagatose: Cloning, overexpression and characterization of L-arabinose isomerase from Pediococcus pentosaceus PC-5
文献类型:期刊论文
作者 | Men, Yan1; Zhu, Yueming1; Zhang, Lili1; Kang, Zhenkui2; Izumori, Ken1; Sun, Yuanxia1; Ma, Yanhe1 |
刊名 | MICROBIOLOGICAL RESEARCH
![]() |
出版日期 | 2014 |
卷号 | 169期号:2-3页码:171-178 |
关键词 | L-Arabinose isomerase D-Tagatose Food-grade microorganisms Pediococcus pentosaceus |
英文摘要 | 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. |
WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
类目[WOS] | Microbiology |
研究领域[WOS] | Microbiology |
关键词[WOS] | THERMAL-STABILITY ; GLUCOSE ISOMERASE ; PROTEIN-STRUCTURE ; ESCHERICHIA-COLI ; SWISS-MODEL ; PH OPTIMUM ; ACIDIC PH ; PURIFICATION ; EXPRESSION ; STRAIN |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000330335600008 |
源URL | [http://124.16.173.210/handle/834782/1409] ![]() |
专题 | 天津工业生物技术研究所_功能糖与天然活性物质研究组 孙媛霞 _期刊论文 |
作者单位 | 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 |
推荐引用方式 GB/T 7714 | Men, Yan,Zhu, Yueming,Zhang, Lili,et al. Enzymatic conversion of D-galactose to D-tagatose: Cloning, overexpression and characterization of L-arabinose isomerase from Pediococcus pentosaceus PC-5[J]. MICROBIOLOGICAL RESEARCH,2014,169(2-3):171-178. |
APA | Men, Yan.,Zhu, Yueming.,Zhang, Lili.,Kang, Zhenkui.,Izumori, Ken.,...&Ma, Yanhe.(2014).Enzymatic conversion of D-galactose to D-tagatose: Cloning, overexpression and characterization of L-arabinose isomerase from Pediococcus pentosaceus PC-5.MICROBIOLOGICAL RESEARCH,169(2-3),171-178. |
MLA | Men, Yan,et al."Enzymatic conversion of D-galactose to D-tagatose: Cloning, overexpression and characterization of L-arabinose isomerase from Pediococcus pentosaceus PC-5".MICROBIOLOGICAL RESEARCH 169.2-3(2014):171-178. |
入库方式: OAI收割
来源:天津工业生物技术研究所
浏览0
下载0
收藏0
其他版本
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。