Abstract
Cellulose hydrolyzing enzyme from fungus Trichoderma viride was purified and characterized. The cellulase production was variable depending upon the type of cellulose the fungus grew on; it was higher when grown on cellulose or whatmann filter paper than on other carbon source viz carboxy methyl cellulose. Enzyme purification to homogeneity was carried out by anion exchange chromatography on DEAE-Sepharose. SDS-PAGE revealed molecular mass of 87 kDa. Maximal activity of the enzymes was observed at 50°C at pH 4 and was stimulated by Ca2+, Co2+, Mg2+ (test at 10 Mm each) and inhibited by Fe2+. Ethanol at an optimum concentration of 2% stimulated the initial enzyme activity. The end product of cellulase action was glucose and cellobiose. The enzyme therefore qualifies as an exo-β 1, 4-glucanase. Thermostability, pH and stability in the presence of surface active agents make this enzyme potentially useful in industry particularly for ethanol production. Key words: Enzyme, cellulose, cellulase.
Highlights
The cellulase production was variable depending upon the type of cellulose the fungus grew on; it was higher when grown on cellulose or whatmann filter paper than on other carbon source viz carboxy methyl cellulose
Cellulose is a linear polymer of up to 15,000 D-glucose residues linked by β (1-4) glycosidic bonds and is an enzyme that hydrolyzes the β-1, 4-glycosidic bonds in cellulose to release glucose units with distinction of being the most abundant component of plant biomass, found exclusively in plant cells and is produced in some bacteria and animals (Nishida et al, 2007)
Half a milliliter of enzyme in 0.1 M Tris-HCl was incubated with 0.5% cellulose solution and 50 μl aliquot withdrawn after every hour to determine the amount of reducing sugars released
Summary
Cellulose is a linear polymer of up to 15,000 D-glucose residues linked by β (1-4) glycosidic bonds and is an enzyme that hydrolyzes the β-1, 4-glycosidic bonds in cellulose to release glucose units with distinction of being the most abundant component of plant biomass, found exclusively in plant cells and is produced in some bacteria and animals (Nishida et al, 2007). A multienzyme complex, components of the cellulose enzymes were first classified on the mode of catalytic action and have been categorized based on the structural properties. Three major types of enzyme activities are found: 1) Endoglucanase; 2) Exoglucanase and 3) β-Glucosidase. These enzymes carry out hydrolysis by the synergistic action (Liming and Xueliang, 2004; Vinha, 2011). The cellulolytic system of filamentous fungus Trichoderma reesei has been studied because of its efficiency in degrading native cellulose substrate (Teeri et al.,1992). The present study aimed the isolation and biochemical characterization of cellulose from Trichoderma for biotechnological application because any process which could efficiently and economically convert celluloytic material to glucose would be of immense industrial significance (Walsh, 2002)
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