Computational investigation of sugar fermentation inhibition by bergenin at the pyruvate decarboxylate isoenzyme 1 target of <em>Scharomyces cervisiae</em>

Abstract

The powdered bark of Sacoglottis gabonensis has been used over the years to improve the shelve life of palm wine. The inhibition of sugar fermentation by bergenin a major phytochemical extract from the bark of this plant at the pyruvate decarboxylate isoenzyme 1 of Saccharomyces cerevisiae was studied using in silico methods. The binding affinity of glucose, fructose, sucrose, maltose, and the natural product bergenin were –3.5 Kcal/mol, –3.4 Kcal/mol, –4.0 Kcal/mol, –4.6 Kcal/mol, and –4.5 Kcal/mol, respectively. Maltose fermentation cannot occur without its hydrolysis to glucose molecules. Since the binding affinity of bergenin is much higher than those of glucose and fructose, then the saturation of the fermentative active sites in pyruvate decarboxylate isoenzyme 1 by this molecule would prevent the occurrence of this reaction. The findings from this study support the age-long practice of increasing the shelf life of freshly tapped palm wine by adding the pulverized bark of S. gabonensis into it.