Isolation and characterization of a thermostable endo-β-glucanase active on 1,3-1,4-β-D-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70

Patrick G. Murray, Alice Grassick, Christopher D. Laffey, Michelle M. Cuffe, Timothy Higgins, Angela V. Savage, Antoni Planas, Maria G. Tuohy

Producción científica: Artículo en revista indizadaArtículorevisión exhaustiva

89 Citas (Scopus)

Resumen

A novel endoglucanase active on 1,3-1,4-β-d-glucans was purified to apparent homogeneity from submerged cultures of the moderately thermophilic aerobic fungus Talaromyces emersonii CBS 814.70. The enzyme is a single subunit glycoprotein with Mr and pI values of 40.7 ± 0.3 kDa and 4.4, respectively, and an estimated carbohydrate content of 77% (w/w). The purified β-glucanase displayed activity over broad ranges of pH and temperature, yielding respective optima values of pH 4.8 and 80°C. This enzyme was markedly thermostable with 15% of the original activity remaining after incubation for 15 min at 100°C. Substrate specificity studies revealed the identity of the enzyme to be a 1,3-1,4-β-d-glucanase. Identical Km values (13.38 mg.ml-1) were obtained with lichenan and BBG, while the Vmax value with lichenan (142.9 IU.mg-1) was approximately twice the value obtained with BBG (79.3 IU.mg-1). Time-course hydrolysis of barley-β-glucan did not proceed linearly with respect to time indicating an 'endo' or more processive action for the enzyme. HPAEC fractionation of the products of hydrolysis yielded a range of oligosaccharides, with cellobiose, cellotriose and cellotetraose being the predominant oligosaccharide products.

Idioma originalInglés
Páginas (desde-hasta)90-98
Número de páginas9
PublicaciónEnzyme and Microbial Technology
Volumen29
N.º1
DOI
EstadoPublicada - 5 jul 2001

Huella

Profundice en los temas de investigación de 'Isolation and characterization of a thermostable endo-β-glucanase active on 1,3-1,4-β-D-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70'. En conjunto forman una huella única.

Citar esto