Purification and characterization of a novel α-glucosidase from Malbranchea cinnamomea.
Biotechnol Lett
; 37(6): 1279-86, 2015 Jun.
Article
em En
| MEDLINE
| ID: mdl-25724718
ABSTRACT
OBJECTIVES:
To characterize a novel α-glucosidase from the thermophilic fungus Malbranchea cinnamomea.RESULTS:
The enzyme was purified to homogeneity with purification fold of 40 and a recovery of 7.2 %. It was a monomer with molecular mass of 65.7 kDa on SDS-PAGE. It was optimally active at pH 6 and 50 °C (measured over 10 min) and exhibited a wide range of substrate specificity with the highest specific activity of 47.4 U mg(-1) for p-nitrophenyl α-D-glucopyranoside (pNPGlu) followed by isomaltose, panose and sucrose, suggesting that the enzyme belongs to the type I α-glucosidases. The K m values of the α-glucosidase for pNPGlu and isomaltose were 1.1 and 19.3 mM, respectively.CONCLUSION:
Because of its unique properties, the α-glucosidase may have a potential in several industrial applications.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Onygenales
/
Alfa-Glucosidases
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article