Abstract
Proteins of a crude enzyme preparation obtained from the cultivation medium of the basidiomycetePhellinus abietis were separated by gel filtration and ion-exchange chromatography. The preparation contained a minimum of three enzymes capable of splitting α-d-mannosidic bonds: α-mannosidase, exomannanase, and endomannanase, which were separated. Some properties of the mannanase complex of the crude enzyme preparation, and of a partially purified α-mannosidase were examined. The mannanase complex exhibited two pH optima, its temperature optimum being at 46 °C The pH optimum of purified α-mannosidase was at pH 5.0, the temperature optimum was at 60 °C; the enzyme had a relatively high heat stability. The Km of α-mannosidase forp-nitrophenyl α-d-mannopyranoside was 1.5 x 10−5 M. Pure α-mannosidase did not split mannan.
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Zouchová, Z., Kocourek, J. & Musílek, V. Separation and properties of α-mannosidase and mannanase from the basidiomycetePhellinus abietis . Folia Microbiol 22, 98–105 (1977). https://doi.org/10.1007/BF02881634
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DOI: https://doi.org/10.1007/BF02881634