National Academy of Agricultural Sciences (NAAS)
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PRINT ISSN : 2319-7692
Online ISSN : 2319-7706 Issues : 12 per year Publisher : Excellent Publishers Email : editorijcmas@gmail.com / submit@ijcmas.com Editor-in-chief: Dr.M.Prakash Index Copernicus ICV 2018: 95.39 NAAS RATING 2020: 5.38 |
Plant wastes could be a potential source of novel pectinases for use in various industrial applications due to their broad substrate specificity with high stability under extreme conditions. Therefore, the application conditions of novel pectinases (Polygalacturonase and Pectin lyase) from Carica papaya cv. solo 8 pericarp were optimized in this study. Those enzymes were partially purified by ammonium sulphate precipitation, dialysis and isoelectric focusing. The polygalacturonase and pectin lyase were partially purified 1.3 and 1.26 fold with a yield approximately 20 % and 24 %, respectively, following purification with isoelectric focusing. The specific activities of 3.62 and 0.176 UI/mg for polygalacturonase and pectin lyase enzymes were calculated, respectively. The optimal pH of 5.0 and 8.0 were obtained for the polygalacturonase and pectin lyase, respectively while an optimal temperature of 45°C was obtained for polygalacturonase and 50 °C for pectin lyase. Polygalacturonase and pectin lyase activities were enhanced by Na+, Ca2+, K+, and Mg2+ while EDTA has any effect at all concentrations on pectin lyase activity whereas EDTA was inhibitory to polygalacturonase activity. The results suggest that Carica papaya pericarp peels can be used for value added synthesis of pectinase, an important enzyme with numerous biotechnological applications.
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