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Purification, characterisation and application of Î±âlârhamnosidase from Penicillium citrinum MTCCâ8897
- Yadav, Sarita, Yadav, Vinita, Yadav, Sudha, Yadav, Kapil D.S.
- International journal of food science & technology 2012 v.47 no.2 pp. 290-298
- Penicillium citrinum, ammonium sulfate, carboxymethylcellulose, chromatography, culture filtrates, enzymes, hesperidin, molecular weight, naringin, odors, pH, polyacrylamide gel electrophoresis, proteins, rutin, sodium sulfate, temperature, wines
- An Î±âlârhamnosidase secreted by Penicillium citrinum MTCCâ8897 has been purified to homogeneity from the culture filtrate of the fungal strain using ammonium sulphate precipitation and cationâexchange chromatography on carboxymethyl cellulose. The sodium dodecyl sulphate/polyacrylamide gel electrophoresis analysis of the purified enzyme gave a single protein band corresponding to the molecular mass 51.0âkDa. The native polyacrylamide gel electrophoresis also gave a single protein band confirming the enzyme purity. The Km and Vmax values of the enzyme for pânitrophenyl Î±âlârhamnopyranoside were 0.36âmm and 22.54âÎ¼moleâminâ1âmgâ1, respectively, and kcat value was 17.1âsâ1 giving kcat/Km value of 4.75âÃâ104âmâ1âsâ1. The pH and temperature optima of the enzyme were 7.0 and 60âÂ°C, respectively. The purified enzyme liberated lârhamnose from naringin, rutin, hesperidin and wine, indicating that it has biotechnological application potential for the preparation of lârhamnose and other pharmaceutically important compounds from natural glycosides containing terminal Î±âlârhamnose and also in the enhancement of wine aroma.