α-l-rhamnosidase selective for rutin to isoquercitrin transformation from Penicillium griseoroseum MTCC-9224.
Bioorg Chem
; 70: 222-228, 2017 02.
Article
em En
| MEDLINE
| ID: mdl-28110962
ABSTRACT
An α-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 α-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 97kDa in SDS-PAGE analysis. The native-PAGE analysis also gave a single protein band confirming the purity of the enzyme. Using p-nitrophenyl-α-l-rhamnopyranoside as the substrate, Km and kcat values of the enzyme were 0.65mM and 43.65s-1, respectively. The pH and temperature optima of the enzyme were 6.5 and 57°C, respectively. The activation energy for the thermal denaturation of the enzyme was 27.9kJ/mol. The purified α-l-rhamnosidase hydrolyzed rutin to isoquercitrin and l-rhamnose but has no effect on naringin and hesperidin.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Penicillium
/
Quercetina
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Rutina
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Glicosídeo Hidrolases
Idioma:
En
Revista:
Bioorg Chem
Ano de publicação:
2017
Tipo de documento:
Article