Purification and properties of the endocellular beta-glucosidase of Candida cacaoi Buckley and Van Uden CBS 2020.
The endocellular enzyme beta-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 60 degrees C. This enzyme was active against soluble glucosides tested with beta(1-2), beta(1-3), beta(1-4) and even alpha(1-4) and alpha(1-6) and was inhibited by D-glucono-delta-lactone. The enzyme was constitutive but its synthesis was repressed by glucose.
Drider
D
D
Chaire de Microbiologie Industrielle et de Génétique des Microorganismes, Ecole Nationale Supérieure Agronomique de Montpellier, France.
Pommares
P
P
Chemardin
P
P
Arnaud
A
A
Galzy
P
P
D002175:Candida / Q000201:enzymology*; D002240:Carbohydrate Sequence; D002412:Cations / Q000494:pharmacology; D004187:Disaccharides / Q000737:chemistry / Q000378:metabolism; D005516:Food Microbiology; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011489:Protein Denaturation; D013379:Substrate Specificity; D014920:Wine; D001617:beta-Glucosidase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism
D002412:Cations; D004187:Disaccharides; D001617:beta-Glucosidase