Abstract
Tannases are a family of esterases that catalyze the hydrolysis of ester and depside bonds of hydrolyzable tannins to release small compounds such as glucose. In this work, tannase production from Bacillus cereus strain KMS3-1 was purified and characterized. The standard methods, such as ammonium sulfate precipitation followed by gel filtration chromatography, were used to purify the enzyme tannase from KMS3-1. With 40% enzyme recovery, the purification process yielded a 1.93-fold increase in specific activity. Analysis using SDS-PAGE confirmed a molecular weight of about 40 kDa. Circular dichroism analysis revealed the secondary structure composition α-helix (12.03%), indicating a dominant role of β-turns (38.4%). A pH of 6.0 and a temperature between 50 and 60 °C were ideal for enzyme activity. Tannic acid has an enzyme Km value of 3.0 x 10−3 M and a Vmax of 4.45 U/mL. Surfactants, metal ions, organic solvents, and inhibitors significantly influence the enzyme activity. Cytotoxicity assays revealed the non-toxic nature of the purified enzyme on Vero cells and rat animal models. These results explore and contribute to a better understanding of tannase enzyme properties and their potential applications in the food and beverage industries.
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