XYLAN AND CARBOXYMETHYLCELLULOSE DIGESTIVE ENZYMES ISOLATED FROM THE ABDOMEN OF THE SMALL SOLDIER OF THE TERMITE MACROTERMES SUBHYALINUS.
Dr. Fagbohoun Jean Bedel*, Yapi Jocelyn Constant, Deffan Kahndo Prudence, Ekissi Gbocho Serge Elvis and Kouame Lucien Patrice
ABSTRACT
By low pressure Chromatographic techniques two isoform enzymes (Ab-CX1 and Ab-CX2) were isolated from the abdomen of the small soldier of the termite Macrotermes subhyalinus. These enzymes are bifunctional because they have the ability to hydrolyze both xylan and carboxymethylcellulose substrates. Their detection by electrophoresis under native conditions revealed a protein band for each. the relative molecular weights determined by SDS-PAGE and gel filtration suggest that the enzyme Ab-CX1 is tetrameric and Ab-CX2 dimeric. The physicochemical characterization of the enzymes Ab-CX1 and Ab-CX2 shows that they are acids with a stability at pH 4.6-5.6. They exhibit maximum activity at a temperature of 50 and 55°C respectively for the enzymes Ab-CX1 and Ab-CX2. The Cu2+ cation have inhibitory effects while Mn2+, Na+, K+. Also, we find that EDTA has no effect on the catalytic activity of these biocatalyses.
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