Abstract
Beta-glucosidase is among the suite of enzymes produced by white rot fungi (WRF) to biodegrade plant biomass. This study investigated the enzymatic activities and kinetic properties of β-glucosidase from seventeen WRF comprised of the following species from various geographical locations: Pleurotus ostreatus, Auricularia auricular, Polyporus squamosus, Trametes versicolor, Lentinula edodes, and Grifola frondosa. All the WRF studied showed β-glucosidase activities. Significant variations in protein and carbohydrate contents were also recorded. Beta-glucosidase activities after 30 min of incubation ranged from 6.4 μg (T. versicolor) to 225 μg (G. frondosa). The calculated kinetic constant (Km) ranged from 0.47 μM (A. auricular-1120) to 719 μM (L. edodes-7). The Vmax depending on the kinetic transformation model ranged from 0.21 μg·min-1 (T. versicolor) to 9.70 μg·min-1 (G. frondosa-28). Beta-glucosidase activities also exhibited pH optima between 3.5 and 5.0 while temperature optima were between 60°C and 70°C with some media exhibiting a secondary temperature peak at 90°C attributable to the presence of thermostable isoenzyme. WRF if appropriately screened and purified can be harnessed to potentially improve the bio-conversion of cellulose to glucose and also facilitate efficient plant biomass biodegradation and production of useful plant bio-products.
Highlights
White rot fungi (WRF) are microorganisms of great in-terest that secrete complex suites of nonspecific extracellular ligninolytic enzymes, i.e., lignin peroxidase (EC 1.11.1.14), manganese peroxidase (EC 1.11.1.13), and laccase (EC 1.10.3.2) to biodegrade lignin [1] or digest substrates required for their proliferation and growth
This study investigated the enzymatic activities and kinetic properties of β-glucosidase from seventeen white rot fungi (WRF) comprised of the following species from various geographical locations: Pleurotus ostreatus, Auricularia auricular, Polyporus squamosus, Trametes versicolor, Lentinula edodes, and Grifola frondosa
WRF have been screened for cellulase production potentials [12,13], but despite the vast amount of knowledge available on their enzymes, much is still to be understood about their specific enzymatic potential activities and kinetic properties
Summary
White rot fungi (WRF) are microorganisms of great in-terest that secrete complex suites of nonspecific extracellular ligninolytic enzymes, i.e., lignin peroxidase (EC 1.11.1.14), manganese peroxidase (EC 1.11.1.13), and laccase (EC 1.10.3.2) to biodegrade lignin [1] or digest substrates required for their proliferation and growth. White rot fungi (WRF) are microorganisms of great in-. The importance of white rot fungi has been noted in medicine [2], biodegradation of environmental wastes [3,4], pollutants [5,6], and in providing protein-rich foods [7]. Enzymes involved with the biodegradation of lignocellulosic plant biomass are those of the “cellulase system”, of which β-glucosidase is a constituent [14]. This is because the complete hydrolysis of cellulose to glucose requires this system of enzymes (cellulases) comprised of endoglucanases, exoglucanases (cellobiohydrolases) and β-glucosidase
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