Purification and Characterization of Pectinase fromPaecilomyces variotii and Its Effect on Bioscouring of Cotton Fabrics and Clarification of Fruit Juices

Abstract

According to Global IndustryAnalysts Inc., the global market for industrial enzymes is forecast newlineto reach US$3.74 billion by the year 2015. Among these enzymes, pectinases are one of the most newlineimportant type of industrial enzymes, and their production accounts for about 10% of the overall newlinemanufacturing of enzyme preparations. The present investigation is to brighten the possibilities of newlineassessing the efficiency of the pectinolytic fungi, Paecilomyces variotii in the production ofpectinase. newlineNative mycoflora from fruit waste disposal area soil was isolated and screened for pectinolytic newlineactivity.Among the number of fungal strains isolated from soils of fruit waste disposal area, only newlinefourshowed predominant pectinolytic activity. Since, Paecilomyces variotii showed remarkedly newlineprominent zone of pectinolytic activity, it was selected as the test fungus for optimization, purification newlineand characterization studies.The test fungus was further confirmed as Paecilomyces variotii by DNA newlinesequencing method (BLAST). The test fungal strain was inoculated in the nutrient medium newline(productionmedium) and was subjected to various pH, temperature, incubation period, different source newlineconcentrations of carbon and nitrogen and different fruit wastes as substrate to assess the optimal newlineproduction of the enzyme.An enhanced enzyme production was observed when 1 percentmaltose newline(carbon source), 3 percent ammonium sulphate (nitrogen source)and 3 percent banana peel waste was newlineused as substrate at a pH of 6.0 andin 40°C temperature. Therefore, pectinase was cultured under newlineoptimizedconditions for the further study (purification, characterization and application on cotton newlinefabricsand fruit juices).The purification of the pectinase was carried out by ammonium newlinesulphateprecipitation, dialysis and chromatographic techniques. The molecular mass of purified protein revealed a distinct band with molecular weight of 60 kDa.