A reducing-end-acting chitinase from Vibrio proteolyticus belonging to glycoside hydrolase family 19
A reducing-end-acting chitinase from Vibrio proteolyticus belonging to glycoside hydrolase family 19
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DOI：
10.1007/s00253-008-1352-2
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发表时间：
2008-03-01
影响因子：
5
通讯作者：
Kitaoka, Motomitsu
中科院分区：
文献类型：
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作者：
Honda, Yuji;Taniguchi, Hajime;Kitaoka, Motomitsu
从溶蛋白弧菌（Vibrio proteolyticus，chi 19）中克隆了一个属于糖苷水解酶家族19的几丁质酶基因。该重组酶（Chi 19）对聚合底物表现出弱活性，而对聚合度大于或等于5的完全N-乙酰化壳寡糖（GlcNAc）（n）表现出相当大的活性。它水解（GlcNAc）（n）在第二个键的位置从还原端的壳寡糖。胶体甲壳素在反应初期的水解产物主要是（GlcNAc）（2）。还原胶态几丁质的水解模式清楚地表明，酶从还原端水解聚合物底物。
A chitinase gene belonging to the glycoside hydrolase family 19 from Vibrio proteolyticus (chi19) was cloned. The recombinant enzyme (Chi19) showed weak activities against polymeric substrates and considerable activities against fully N-acetylated chitooligosaccharides, (GlcNAc)(n) , whose degree of polymerization was greater than or equal to five. It hydrolyzed (GlcNAc) (n) at the second linkage position from the reducing ends of the chitooligosaccharides. The hydrolytic products of colloidal chitin were mainly (GlcNAc)(2) from the initial stage of the reaction. The hydrolytic pattern of reduced colloidal chitin clearly suggested that the enzyme hydrolyzed the polymeric substrate from the reducing end.