PMID: 11330684May 2, 2001Paper

Purification and characterization of mannose isomerase from Agrobacterium radiobacter M-1

Bioscience, Biotechnology, and Biochemistry
J HiroseY Takasaki

Abstract

A mannose isomerase from Agrobacterium radiobacter M-1 (formerly Pseudomonas sp. MI) was purified to electrophoretic homogeneity and characterized. A cell-free extract was separated by ammonium sulfate fractionation, Butyl-Toyopearl 650M, DEAE-Sepharose and hydroxylapatite column chromatography. Its molecular mass was estimated to be 44 kDa by SDS-PAGE and 90 kDa by gel filtration, in which the enzyme is most likely a dimer composed of two identical subunits. The purified enzyme had an optimum pH at 8.0, an optimum temperature at 60 degrees C, a pI of 5.2 and a Km of 20 mM, and specifically converted D-mannose and D-lyxose to ketose. The N-terminal amino acid sequence was identified.

Citations

Dec 26, 2006·Journal of Bacteriology·Eun-Ah ChoYu-Ryang Pyun
Jul 8, 2015·Applied Microbiology and Biotechnology·Wanmeng MuBo Jiang
Jul 10, 2010·Journal of Molecular Biology·Laura M van StaalduinenZongchao Jia
Mar 24, 2018·Journal of the Science of Food and Agriculture·Jiawei HuangWanmeng Mu
Jul 4, 2018·Applied Microbiology and Biotechnology·Zheng FangWanmeng Mu
Oct 23, 2019·Applied Microbiology and Biotechnology·Hao WuWanmeng Mu
Nov 3, 2020·Acta Crystallographica. Section D, Structural Biology·Yinghui FengRuijin Yang
Jan 24, 2021·Applied Biochemistry and Biotechnology·Xiaohan HuaQiaojuan Yan
Jul 1, 2016·Comprehensive Reviews in Food Science and Food Safety·Xing HuBo Jiang

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