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Purification and properties of the β‐glucosidase of a new strain of Candida molischiana able to work at low pH values: Possible use in the liberation of bound terpenols
Author(s) -
Vasserot Yann,
Chemardin Patrick,
Arnaud Alain,
Galzy Pierre
Publication year - 1991
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.3620310413
Subject(s) - yeast , enzyme , size exclusion chromatography , strain (injury) , sodium dodecyl sulfate , glucosyltransferase , chemistry , chromatography , enzyme assay , ethanol , specific activity , biochemistry , sodium , liberation , protein subunit , biology , in vitro , organic chemistry , gene , anatomy
A yeast strain isolated in the laboratory was studied and classified as a Candida molischiana. The β‐glucosidase of this yeast strain was then purified. Its molecular weight, estimated by gel filtration, was 100,000. The enzyme consisted of only one subunit, identified after treatment with sodium dodecyl sulfate. Maximum activity was obtained at 55°C and pH 4 but the enzyme still possessed activity at pH 2.5. Active against different glucosides with β(1–2), β(1–3), β(1–4), β(1–6), and α(1–4) configurations it presented an α(1–6)‐arabinofuranosidase activity. The enzyme was competitively inhibited by glucose ( K i 9. 5 mm). A glucosyltransferase activity appeared in the presence of ethanol. The enzyme was constitutive but its synthesis was repressed by glucose.