Pectin Degradation In Fruit Juices By Pectinase From Meyerozyma Sp. Vitpct75 Isolated From Phyllanthus Emblica

This study aimed to identify and characterize a pectinase-producing novel yeast from the fermented juice of Phyllanthus emblica and apply the enzyme for fruit juice clarification. Among the five pectinase-producing yeasts, isolate-1 exhibited the highest pectinase activity and was further used in this study. Based on morphological, physiological, and 18SrRN Aanalyses, isolate-1 was recognized as a new strain sharing 99% sequence homology with other Meyerozyma strains and was thus designated as Meyerozyma sp. VITPCT75. The strain produced pectinase optimally at a temperature and pH of 25 degrees C and 7, respectively. Maximum pectinase production was observed after 4-days incubation. The enzyme exhibited optimum activity at the temperature of 25 degrees C and pH 7.0. The enzyme was more stable at a temperature and pH of 20 degrees C and 7, respectively. Storage stability studies revealed that the enzyme was stable at -20 degrees C. The cell-free supernatant was partially purified using ammonium sulfate and solvent precipitation. Acetone at a concentration of 20% assured an adequate partial purification. The molecular weight of pectinase was determined as 6 kDa. The enzymatic metal ion preference-related studies revealed that Ca(2)z, Kz, Cu(2)z, Fez, and Baez ions enhanced, Ni(2)z ions moderately inhibited, and Mn(2)z ions intensely inhibited the enzymatic activity. Neither Na+ and Me2+ ions nor EDTA affected the enzyme activity. When subjected to fruit juice clarification, the enzyme significantly reduced the viscosity of the juice.