Cervone F, Scala A, Noviello C
Ital J Biochem. 1977 Jan-Feb;26(1):59-68.
A pectolytic enzyme from culture filtrates of Rhizoctonia fragariae was purified approx. 29-fold. The enzyme exhibited maximal depolymerizing activity on Na-polypectate rather than pectin at pH 5.0 and was inhibited at different extent by divalent cations Mg++, Mn++, Ca++. The analysis by paper chromatography of the products of enzyme hydrolysis suggested that the enzyme attacks the substrate by a random mechanism. The absorption spectrum of the chromogen formed by the hydrolysis products and thiobarbituric acid suggested that the enzyme is a hydrolytic enzyme. On the basis of these results the enzyme is classifiable as endo-polygalacturonase (poly alpha-1,4-galacturonide glycanohydrolase E.C. 3.2.1.15).
从草莓丝核菌培养滤液中分离得到一种果胶酶,纯化了约29倍。该酶在pH 5.0时对聚半乳糖醛酸钠而非果胶表现出最大解聚活性,并受到二价阳离子Mg++、Mn++、Ca++不同程度的抑制。酶水解产物的纸层析分析表明,该酶以随机机制作用于底物。水解产物与硫代巴比妥酸形成的色原的吸收光谱表明该酶是一种水解酶。基于这些结果,该酶可归类为内切聚半乳糖醛酸酶(聚α-1,4-半乳糖醛酸聚糖水解酶,E.C. 3.2.1.15)。