National Academy of Agricultural Sciences (NAAS)
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PRINT ISSN : 2319-7692
Online ISSN : 2319-7706 Issues : 12 per year Publisher : Excellent Publishers Email : editorijcmas@gmail.com / submit@ijcmas.com Editor-in-chief: Dr.M.Prakash Index Copernicus ICV 2018: 95.39 NAAS RATING 2020: 5.38 |
An alkali tolerant α-L-rhamnosidase from the culture filtrate of a fungal strain, Fusarium poae MTCC-2086 has been purified to homogeneity. The procedure involved concentration by ultrafiltration and cation-exchange chromatography on carboxymethyl cellulose. The purified enzyme gave a single protein band corresponding to molecular mass of 51.0 kDa in SDS-PAGE analysis showing that the enzyme preparation was pure. The native PAGE analysis of the purified enzyme also gave single protein band confirming the purity of the enzyme preparation. Using p-nitrophenyl -α-L-rhamnopyranoside as substrate, Km and kcat values of the enzyme were 0.49 mM and 30.4s-1, respectively. The pH and temperature optima of the enzyme were 10.0 and 55 °C, respectively. The enzyme is stable below 10ºC and at pH 10.0. The energy of activation for thermal denaturation of enzyme determined by Arrhenius plot was 26.06 k J mol-1.The enzyme hydrolysed hesperidin to L-rhamnose and hesperitin-7-O-glucoside but it did not hydrolyse naringin and rutin.
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