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Purification and properties of the endocellular β‐glucosidase of Candida cacaoi Buckley and Van Uden CBS 2020
Author(s) -
Drider D.,
Pommares P.,
Chemardin P.,
Arnaud A.,
Galzy P.
Publication year - 1993
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1993.tb05156.x
Subject(s) - enzyme , size exclusion chromatography , chemistry , chromatography , ion chromatography , enzyme assay , stereochemistry , biochemistry
D. DRIDER, P. POMMARES, P. CHEMARDIN, A. ARNAUD AND P. GALZY. 1993. The endocellular enzyme β‐glucosidase of Candida cacaoi was purified by ion‐exchange chromatography and gel filtration. The molecular weight was 220 ± 10 kDa; its optimum pH was between 4 and 5.5 and its optimum temperature was 60d̀C. This enzyme was active against soluble glucosides tested with β(1–2), β(1–3), β(1–4) and even α(1–4) and α(1–6) and was inhibited by D‐glucono‐δ‐lactone. The enzyme was constitutive but its synthesis was repressed by glucose.