对鞘氨醇单胞菌CJ-5产生的几丁质酶和壳聚糖酶的分析。
Analysis of both chitinase and chitosanase produced by Sphingomonas sp. CJ-5.
作者信息
Zhu Xu-Fen, Zhou Ying, Feng Jun-Li
机构信息
College of Life Science, Zhejiang University, Hangzhou, China.
出版信息
J Zhejiang Univ Sci B. 2007 Nov;8(11):831-8. doi: 10.1631/jzus.2007.B0831.
Abstract
A novel chitinolytic and chitosanolytic bacterium, Sphingomonas sp. CJ-5, has been isolated and characterized. It secretes both chitinase and chitosanase into surrounding medium in response to chitin or chitosan induction. To characterize the enzymes, both chitinase and chitosanase were purified by ammonium sulfate precipitation, Sephadex G-200 gel filtration and DEAE-Sepharose Fast Flow. SDS-PAGE analysis demonstrated molecular masses of chitinase and chitosanase were 230 kDa and 45 kDa respectively. The optimum hydrolysis conditions for chitinase were about pH 7.0 and 36 degrees C, and these for chitosanase were pH 6.5 and 56 degrees C, respectively. Both enzymes were quite stable up to 45 degrees C for one hour at pH 5~8. These results show that CJ-5 may have potential for industrial application particularly in recycling of chitin wastes.
摘要
一种新型的几丁质分解和壳聚糖分解细菌，鞘氨醇单胞菌属CJ-5，已被分离和鉴定。它在几丁质或壳聚糖诱导下，会向周围培养基中分泌几丁质酶和壳聚糖酶。为了鉴定这些酶，通过硫酸铵沉淀、Sephadex G-200凝胶过滤和DEAE-琼脂糖快速流动法对几丁质酶和壳聚糖酶进行了纯化。SDS-PAGE分析表明，几丁质酶和壳聚糖酶的分子量分别为230 kDa和45 kDa。几丁质酶的最佳水解条件约为pH 7.0和36℃，壳聚糖酶的最佳水解条件分别为pH 6.5和56℃。在pH 5至8时，两种酶在45℃下保温1小时都相当稳定。这些结果表明，CJ-5在工业应用方面，特别是在几丁质废物回收利用方面可能具有潜力。
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