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JOURNAL ARTICLE
RESEARCH SUPPORT, NON-U.S. GOV'T
Interaction of microbial β-glucuronidase with vegetable pectins.
Journal of Agricultural and Food Chemistry 2011 September 29
The purpose of this study was to investigate the in vitro effects of vegetable carbohydrates on the activity of microbial β-glucuronidase (βG) and the adsorption of the enzyme on carbohydrates. This study used pectin-protein complexes (PPCs) with molecular weights of 300 kDa isolated under conditions simulating a gastric environment from cabbage (HCl-PPCC and HCl+pepsin-PPCCP) and sweet pepper (PPCP and PPCPP). As a sample for comparison, microcrystalline cellulose was used. The activity of βG from Escherichia coli was determined spectrophotometrically by the formation of the colored product from the breakdown of phenolphthalein-β-D-glucuronide. Adsorption of βG on biopolymers was studied by the retention of the enzyme on the membrane of a concentrator with a pore diameter of 300 kDa and by native PAGE. PPCCP and PPCC were established to increase the activity of βG by 50 and 100%, respectively. Cellulose had a weak effect, whereas pepper PPC had no effect. All studied carbohydrates adsorb on βG. The maximum βG adsorption (15%) was observed with PPCC, whereas PPCCP absorbed 5% of the enzyme. Pepper PPCs and cellulose adsorbed up to 10% of the enzyme. There was a positive correlation between the increase of βG activity in the presence of carbohydrates and enzyme adsorption on the polymers (r=0.80; P<0.01). The activity of the enzyme in the gel after electrophoresis of the PPCC+βG mixture was inversely proportional to the concentration of PPCC in the mixture. A model explaining the effects of cabbage PPCs on the excretion of estrogens is proposed.
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