We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Membrane-bound D-mannose isomerase of acetic acid bacteria: finding, characterization, and application.
- Authors
Osao Adachi; Naoya Kataoka; Kazunobu Matsushita; Yoshihiko Akakabe; Toshihiro Harada; Toshiharu Yakushi
- Abstract
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.
- Subjects
ACETOBACTER; ISOMERASES; IMMOBILIZED cells; MOLECULAR weights; CELL fractionation; FRUCTOSE
- Publication
Bioscience, Biotechnology & Biochemistry, 2022, Vol 86, Issue 7, p938
- ISSN
0916-8451
- Publication type
Article
- DOI
10.1093/bbb/zbac049