Membrane-bound<scp>d</scp>-mannose isomerase of acetic acid bacteria: finding, characterization, and application
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- Osao Adachi
- Graduate School of Science and Technology for Innovation, Yamaguchi University , Yamaguchi, Japan
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- Naoya Kataoka
- Graduate School of Science and Technology for Innovation, Yamaguchi University , Yamaguchi, Japan
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- Kazunobu Matsushita
- Graduate School of Science and Technology for Innovation, Yamaguchi University , Yamaguchi, Japan
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- Yoshihiko Akakabe
- Graduate School of Science and Technology for Innovation, Yamaguchi University , Yamaguchi, Japan
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- Toshihiro Harada
- Harada Foods Co. , Ltd., Yanai, Japan
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- Toshiharu Yakushi
- Graduate School of Science and Technology for Innovation, Yamaguchi University , Yamaguchi, Japan
書誌事項
- 公開日
- 2022-06-16
- 資源種別
- journal article
- 権利情報
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- https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model
- DOI
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- 10.1093/bbb/zbac049
- 公開者
- Oxford University Press (OUP)
説明
<jats:title>ABSTRACT</jats:title><jats:p>d-Mannose isomerase (EC 5.3.1.7) catalyzing reversible conversion between d-mannose and d-fructose was found in acetic acid bacteria. Cell fractionation confirmed the enzyme to be a typical membrane-bound enzyme, while all sugar isomerases so far reported are cytoplasmic. The optimal enzyme activity was found at pH 5.5, which was clear contrast to the cytoplasmic enzymes having alkaline optimal pH. The enzyme was heat stable, and the optimal reaction temperature was observed at around 40-60 °C. Purified enzyme after solubilization from membrane fraction showed the total molecular mass of 196 kDa composing of identical 4 subunits of 48 kDa. Washed cells or immobilized cells were well functional at nearly 80% of conversion ratio from d-mannose to d-fructose and reversely 20%-25% of d-fructose to d-mannose. Catalytic properties of the enzyme were discussed with respect to the biotechnological applications to high fructose syrup production from konjac taro.</jats:p>
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 86 (7), 938-948, 2022-06-16
Oxford University Press (OUP)