alpha-L-rhamnosidase from Aspergillus clavato-nanicus MTCC-9611 active at alkaline pH

作者:Yadav Vinita*; Yadav Saroj; Yadav Sarita; Yadav K D S
来源:Applied Biochemistry and Microbiology, 2012, 48(3): 295-301.
DOI:10.1134/S0003683812030155

摘要

An a-L-rhamnosidase secreting fungal strain has been isolated and identified as Aspergillus clavato-nanicus MTCC-9611. The enzyme was purified to homogeneity from the culture filtrate of the fungus using concentration by ultrafiltration membrane and ion-exchange chromatography on CM-cellulose. The native PAGE analysis confirmed the homogeneity of the purified enzyme. The SDS-PAGE analysis of the purified enzyme revealed a single protein band corresponding to the molecular weight 82 kDa. The alpha-L-rhamnosidase activity of Aspergillus clavato-nanicus MTCC-9611 had optimum at pH 10.0 and 50A degrees C. The K (m) values of the enzyme were 0.65 mM and 0.95 mM using p-nitrophenyl alpha-L-rhamnopyranoside and naringin as a substrates respectively. The enzyme transforms naringin to prunin at pH 10.0 and further hydrolysis of prunin to naringenin does not occur under these reaction conditions that makes alpha-L-rhamnosidase activity of Aspergillus clavato-nanicus MTCC-9611 promising enzyme to get prunin for pharmaceutical purposes.

  • 出版日期2012-5

全文