Purification and biochemical characterization of β‐d‐fructofuranosidase from Bacillus subtilis LYN12

AbstractThe purification and biochemical characterization of extracellular β‐d‐fructofuranosidase fromBacillus subtilis LYN12 was carried out. The enzyme was purified 6.94 folds over the crude extract by gel filtration chromatography with recovery of 15.58%. The molecular mass of ∼66 kDa estimated by SDS‐PAGE was confirmed by LC‐MS as 64512.31 Da. Bacterial β‐d‐fructofuranosidase was found to be a glycoprotein with 62.64% carbohydrate content, and exhibited enhanced activities at broad pH, temperature and stable at pH 7.0, 40°C, respectively. The enzyme showed high affinity ford‐sucrose. Kinetic parametersKm andVmax were 41.98  mM and 1.184 µmol/min, respectively. β‐d‐fructofuranosidase activity was inhibited by the divalent metal ions Cu2+ and Hg2+, whereas improved by Mg2+, Fe2+ and few sulphydryl group reagents. β‐d‐fructofuranosidase demonstrated ethanol tolerance up to 15% with 76.4% of activity.B. subtilis LYN12 invertase is suggested as a potential enzyme with suitable characteristics for numerous industrial applications.Practical applicationsβ‐d‐fructofuranosidases are one of the industrially important carbohydrases utilized in many applications such as beverages, baking, confectionaries, nutraceuticals and also medicinal formulations. The production of β‐d‐fructofuranosidase fromBacillus subtilis LYN12 by solid ‐state fermentation demonstrates the utilization of agro‐industrial wastes, such as wheat bran and molasses. T...

Source: Journal of Food Biochemistry - October 24, 2018 Category: Food Science Authors: Lynette Lincoln, Sunil S. More, Shwetha V. Reddy Tags: FULL ARTICLE Source Type: research