Pectinesterase was purified from the culture medium of Aspergilhs juponicus completely free from pectin depolymerizing enzymes. The purified enzyme was able to convert high-methoxyl pectin into lowmethoxyl pectin capable of forming strong gels with calcium ion. The maximum gel strength of enzyme-demethylated pectin was obtained at methoxyl content of 6.3%, calcium concentration of 41.8 mg/g of pectin and pH 3.5. The low-methoxyl pectin, however, formed weaker gels at low concentrations of calcium ion and low pH. DEAE-cellulose column chromatography indicated that the enzyme-demethylated pectin was homogeneous with respect to methoxyl groups of the molecules. It was suggested that this homogeneity may be probably responsible for high gel strength of the lowmethoxyl pectin.
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