alpha-L-rhamnosidase selective for rutin to isoquercitrin transformation from Penicillium griseoroseum MTCC-9224

作者：Yadav Sarita; Yadava Sudha; Yadav Kapil D S

来源：Bioorganic Chemistry, 2017, 70: 222-228.

DOI：10.1016/j.bioorg.2017.01.002

• Penicillium griseoroseum
• Glycoside hydrolase
• Emblica officinalis
• Rutin
• Isoquercitrin

An alpha-L-rhamnosidase secreting fungal strain has been isolated from the decaying goose berry (Emblica officinalis) fruit peel. The fungal strain has been identified as Penicillium greoroseum MTCC-9224. The alpha-L-rhamnosidase of this fungal strain has been purified to homogeneity using a simple procedure involving concentration by ultra filtration and an anion exchange chromatography on DEAE-cellulose. The purified enzyme gave a single protein band corresponding to molecular mass of 97 kDa in SDS-PAGE analysis. The native-PAGE analysis also gave a single protein band confirming the purity of the enzyme. Using p-nitrophenyl-alpha-L-rhamnopyranoside as the substrate, K-m and k(cat) values of the enzyme were 0.65 mM and 43.65 s(-1), respectively. The pH and temperature optima of the enzyme were 6.5 and 57 degrees C, respectively. The activation energy for the thermal denaturation of the enzyme was 27.9 kJ/mol. The purified alpha-L-rhamnosidase hydrolyzed rutin to isoquercitrin and L-rhamnose but has no effect on naringin and hesperidin.

• 出版日期2017-2