Isolation, Characterization, and Molecular Cloning of a Thermostable Xylitol Oxidase from Streptomyces sp.IKD472

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概要

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• A thermophilic bacterium, Streptomyces sp.IKD472, that can oxidize xylitol was isolated from a hot spring and was found to produce xylitol oxidase. The purified enzyme was a monomeric protein with an apparent molecular weight of 43 k as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis and gel filtration. This novel enzyme is capable of catalyzing the oxidation of one mole of xylitol to form one mole each of xylose and hydrogen peroxide. Since the V_<max>/K_m value for xylitol was two and four times higher than those for galactitol and _D-sorbitol, respectively, the enzyme was designated as xylitol oxidase. The enzyme was stable in the pH range from 5.5 to 10.5 and at temperatures up to 65℃. The optimal temperature and pH were 55℃ and pH 7.5, respectively. Xylitol oxidase bound one mole of FAD as a coenzyme per mole of protein. The amino acid sequence of the NH_2 terminus and the fragments obtained by lysylendpeptidase digestion of xylitol oxidase were determined for preparation of synthetic oligonucleotides as hybridization probes. A 2.8-kb chromosomal fragment hybridazing to the probes was cloned into pUC18 in Escherichia coli. The gene consists of an open reading frame of 1245 bp that encodes a protein containing 415 amino acids with a molecular weight of 44, 730 but without the conserved nucleotide-binding sequence, Gly-X-Gly-X-X-Gly. The amino acid sequence has 70% identity to putative oxidoreductase from Streptomyces coelicolar, 51% to sorbitol oxidase from Streptomyces sp., and 26% to _L-gulonolactone oxidase from rat in terms of the overall amino acid sequence. DNA manipulation of the cloned gene in E.coli, by alteration of a strong promoter and a synthesized ribosomebinding sequence at an appropriate position, resulted in overproduction of xylitol oxidase 100 times more than that produced in the original Streptomyces sp.IKD472. The enzyme properties of recombinant xylitol oxidase were the same as those of the authentic enzyme. Stable xylitol oxidases, which allow easier quantitative analysis of xylitol, are useful for clinical applications.

• 社団法人日本生物工学会の論文
• 2000-04-25

著者

• YAMASHITA MITSUO

  Department of Agricultural Chemistry, Faculty of Bioresources, Mie University, Department of Biotech

• MUROOKA YOSHIKATSU

  Department of Agricultural Chemistry, Faculty of Bioresources, Mie University, Department of Biotech

• Furuya Y

  Ikeda Tohka Ind. Co. Ltd. Hiroshima Jpn

• Furuya Yuji

  Research Laboratory Ikeda Food Research Co. Ltd.

• Furuya Yuji

  Ikeda Food Research Co.ltd.

• OMURA Hironori

  Ikeda Food Research Co., Ltd.

• OKAMOTO ERI

  Ikeda Food Research Co.Ltd.

• YABUUCHI MASAHIKO

  Nippon Kayaku Co.Ltd.

• FUKAHI KIMI

  Department of Biotechnology, Graduate School of Engineering, Osaka University

• Fukahi Kimi

  Department Of Biotechnology Graduate School Of Engineering Osaka University

• Omura Hironori

  Ikeda Food Research Co.ltd.

• Omura Hironori

  Ikeda Food Research Co. Ltd.

• Murooka Yoshikatsu

  Depart. Of Bioteclnology Graduate School Of Eng. Osaka Univ.

• Yamashita Mitsuo

  Department Of Agricultural Chemistry Faculty Of Bioresources Mie University Department Of Biotechnol

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