Purification of a soluble and a wall-bound form of beta-glucosidase from Mucor racemosus.
AUTOR(ES)
Borgia, P I
RESUMO
beta-Glucosidase activity in crude extracts of Mucor racemosus exists in a soluble form and in a wall-bound form which sediments at 3,500 x g. The soluble form and a wall-bound form were purified to homogeneity by ammonium sulfate fractionation. DEAE-Sephadex chromatography, and SP-Sephadex chromatography. Both forms were identical in all parameters measured. Each enzyme is a glycoprotein of 91,000 daltons, with an identical amino acid composition and N-terminal amino acid of lysine; both contain about 10% carbohydrate. Both forms catalyze the hydrolysis of cellobiose and p-nitrophenyl-beta-D-glucoside with identical kinetic constants.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=216536Documentos Relacionados
- Control of beta-glucosidase synthesis in Mucor racemosus.
- Isolation and properties of beta-glucosidase from Ruminococcus albus.
- Purification and characterization of a developmentally regulated carboxypeptidase from Mucor racemosus.
- DNA sequence of a beta-glucosidase from Ruminococcus albus.
- Production, purification, and characterization of a highly glucose-tolerant novel beta-glucosidase from Candida peltata.