Purification and Some Properties of α-Mannosidase
Shigeyoshi Katohda, Yasuo Sawaya, Keiji Asatsuma, Fumiko Suzuki, Masaya Hayashibe
Abstract
Shigeyoshi Katohda, Yasuo Sawaya, Keiji Asatsuma, Fumiko Suzuki, Masaya Hayashibe
Abstract
A soil microorganism which was capable of growing in a medium containing baker’s yeast cells as a carbon source was isolated and identified as Acinetobacter sp. When grown in a medium containing baker’s yeast cells, the organism secreted β-l, 6-glucanase, β-1, 3-glucanase and α-mannosidase into the culture medium. Several peaks showing α-mannosìdase activity appeared in DEAE-Sephadex A-50 column chromatography. One of α-mannosidase components showing the highest activity was purified 34-fold over the culture fluid. The enzyme was active on Saccharomyces cerevisiae mannan and some of oligosaccharides produced by the acetolysis of yeast mannan. From the action patterns against these carbohydrates, conclusion being reached, the enzyme is α-1, 2-mannosidase splitíng α-1, 2-mannosyl linkage from non-reducing end.
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A soil microorganism which was capable of growing in a medium containing baker’s yeast cells as a carbon source was isolated and identified as Acinetobacter sp. When grown in a medium containing baker’s yeast cells, the organism secreted β-l, 6-glucanase, β-1, 3-glucanase and α-mannosidase into the culture medium. Several peaks showing α-mannosìdase activity appeared in DEAE-Sephadex A-50 column chromatography. One of α-mannosidase components showing the highest activity was purified 34-fold over the culture fluid. The enzyme was active on Saccharomyces cerevisiae mannan and some of oligosaccharides produced by the acetolysis of yeast mannan. From the action patterns against these carbohydrates, conclusion being reached, the enzyme is α-1, 2-mannosidase splitíng α-1, 2-mannosyl linkage from non-reducing end.
Key concepts: Mannosidase, Mannan, Chemistry, Yeast, Enzyme, Sephadex, Biochemistry, Mannose