Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10146495 | Bioresource Technology | 2018 | 34 Pages |
Abstract
A halotolerant endoglucanase with a molecular mass of 39â¯kDa was obtained from the solid fermentation of sugarcane bagasse by the fungus Botrytis ricini URM 5627 and isolated using only two purification processes: fractionation with ammonium sulphate and size-exclusion chromatography resulting in an activity of 1289.83â¯U/mL. After the isolation, biochemical characterizations were performed, giving a temperature of 50â¯Â°C and optimum pH of 5. The enzyme was stable at 39-60â¯Â°C for 60â¯min and at a pH of 4-6. The enzymatic activity increased in the presence of Na+, Mn2+, Mg2+ and Zn2+ and decreased in the presence of Ca2+, Cu2+, and Fe2+. The endoglucanase revealed a halotolerant profile since its activity increased proportionally to an increase in NaCl concentration. The maximum activity was reached at 2â¯M NaCl with a 75% increase in activity. The enzyme had a Km of 0.1299â¯Â±â¯0.0096â¯mg/mL and a Vmax of 0.097â¯Â±â¯0.00121â¯mol/min/mL. During application in saccharification tests, the enzyme was able to hydrolyse sugarcane bagasse, rice husk, and wheat bran, with the highest production of reducers/fermentable sugars within 24â¯h of saccharification for wheat bran (137.21â¯mg/g). Therefore, these properties combined make this isolated enzyme a potential candidate for biotechnological and industrial applications.
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Authors
Tatielle P. Silva, Fabiana S. de Albuquerque, Cláudio Willian V. dos Santos, Marcelo Franco, Luiz Carlos Caetano, Hugo Juarez Vieira Pereira,