Purification and properties of the beta-glucosidase from a nitrile hydratase-producing Brevibacterium sp. strain R312.
Besides its nitrile hydratase and wide spectrum amidase activities, the Brevibacterium sp. R312 strain also possesses a constitutive beta-glucosidase. Its optimum pH is 6. The enzyme was purified by fractionation precipitation with ammonium sulfate followed by chromatographic elutions on Q-Sepharose Fast Flow, Sephadex G-200 and Phenyl Superose. The resulting purification was 1960 folds for a 6% yield. The molecular weight of this enzyme was estimated at 180,000. It contains two identical sub-units. The pI is 5.5. This enzyme has a strong affinity for aryl-beta-glycosides:pNPG, prunassine; it could also degrade linamarine. It is inhibited by p-chloromercuribenzoate, delta-gluconolactone and glucose.
Legras
J L
JL
Chaire de Génétique et Microbiologie, Ecole Nationale Supérieure Agronomique, Montpellier, France.
Kaakeh
M R
MR
Arnaud
A
A
Galzy
P
P
D001951:Brevibacterium / Q000201:enzymology*; D005591:Chemical Fractionation; D011232:Chemical Precipitation; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D005959:Glucosidases / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008970:Molecular Weight; D012988:Soil Microbiology; D013379:Substrate Specificity; D001617:beta-Glucosidase / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism
D005959:Glucosidases; D001617:beta-Glucosidase