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Biochemical Characterization of an Extracellular beta-Glucosidase from the Fungus, Penicillium italicum, Isolated from Rotten Citrus Peel
Mycobiology ; : 173-180, 2012.
Artigo em Inglês | WPRIM | ID: wpr-729671
ABSTRACT
A beta-glucosidase from Penicillium italicum was purified with a specific activity of 61.8 U/mg, using a chromatography system. The native form of the enzyme was an 88.5-kDa tetramer with a molecular mass of 354 kDa. Optimum activity was observed at pH 4.5 and 60degrees C, and the half-lives were 1,737, 330, 34, and 1 hr at 50, 55, 60, and 65degrees C, respectively. Its activity was inhibited by 47% by 5 mM Ni2+. The enzyme exhibited hydrolytic activity for p-nitrophenyl-beta-D-glucopyranoside (pNP-Glu), p-nitrophenyl-beta-D-cellobioside, p-nitrophenyl-beta-D-xyloside, and cellobiose, however, no activity was observed for p-nitrophenyl-beta-D-lactopyranoside, p-nitrophenyl-beta-D-galactopyranoside, carboxymetyl cellulose, xylan, and cellulose, indicating that the enzyme was a beta-glucosidase. The kcat/Km (s-1 mM-1) values for pNP-Glu and cellobiose were 15,770.4 mM and 6,361.4 mM, respectively. These values were the highest reported for beta-glucosidases. Non-competitive inhibition of the enzyme by both glucose (Ki = 8.9 mM) and glucono-delta-lactone (Ki = 11.3 mM) was observed when pNP-Glu was used as the substrate. This is the first report of non-competitive inhibition of beta-glucosidase by glucose and glucono-delta-lactone.
Assuntos

Texto completo: DisponíveL Índice: WPRIM (Pacífico Ocidental) Assunto principal: Penicillium / Celobiose / Celulose / Cromatografia / Citrus / Beta-Glucosidase / Celulases / Fungos / Glucose / Glucosídeos Idioma: Inglês Revista: Mycobiology Ano de publicação: 2012 Tipo de documento: Artigo

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Texto completo: DisponíveL Índice: WPRIM (Pacífico Ocidental) Assunto principal: Penicillium / Celobiose / Celulose / Cromatografia / Citrus / Beta-Glucosidase / Celulases / Fungos / Glucose / Glucosídeos Idioma: Inglês Revista: Mycobiology Ano de publicação: 2012 Tipo de documento: Artigo