Purification and characterization of an exo-polygalacturonase secreted by Rhizopus oryzae MTCC 1987 and its role in retting of Crotalaria juncea fibre
作者： Sangeeta Yadav , Gautam Anand , Amit Dubey , Dinesh Yadav
DOI: 10.2478/S11756-012-0122-X
关键词:
摘要: An acidic polygalacturonase (PG) secreted by Rhizopus oryzae MTCC-1987 in submerged fermentation condition has been purified to electrophoretic homogeneity using ammonium sulphate fractionation and anion exchange chromatography on diethylaminoethyl cellulose. The enzyme gave a single protein band sodium dodecyl sulphatepolyacrylamide gel electrophoresis analysis with molecular mass corresponding 75.5 kDa. K m k cat values of the PG were 2.7 mg/mL 2.23 × 103 s−1, respectively, citrus polygalacturonic acid as substrate. optimum pH was 5.0 it does not loose activity appreciably if left for 24 hours range from 12.0. temperature 50°C below 30°C exposed two hours. showed complete inhibition 1 mM Ag+, Hg2+ KMnO4, while stimulated some extent Co2+. exhibited retting Crotalaria juncea fibre absence ethylenediaminetetraacetic acid.
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