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2
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Biotechnol Lett. 2006 Sep;28(17):1393-9. doi: 10.1007/s10529-006-9101-z. Epub 2006 Jul 4.
3
Comparison of enzymatic and antifungal properties between family 18 and 19 chitinases from S. coelicolor A3(2).天蓝色链霉菌A3(2)中18家族和19家族几丁质酶的酶学性质与抗真菌特性比较
Biosci Biotechnol Biochem. 2006 Apr;70(4):988-98. doi: 10.1271/bbb.70.988.
4
Role of Chitin-Binding Proteins in the Specific Attachment of the Marine Bacterium Vibrio harveyi to Chitin.几丁质结合蛋白在海洋细菌哈维氏弧菌特异性附着几丁质中的作用。
Appl Environ Microbiol. 1993 Feb;59(2):373-9. doi: 10.1128/aem.59.2.373-379.1993.
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Distribution and phylogenetic analysis of family 19 chitinases in Actinobacteria.放线菌中19家族几丁质酶的分布及系统发育分析
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6
The Saccharomyces cerevisiae chitinase, encoded by the CTS1-2 gene, confers antifungal activity against Botrytis cinerea to transgenic tobacco.由CTS1-2基因编码的酿酒酵母几丁质酶赋予转基因烟草对灰葡萄孢的抗真菌活性。
Transgenic Res. 2003 Aug;12(4):497-508. doi: 10.1023/a:1024220023057.
7
Fermentation conditions and properties of a chitosanase from Acinetobacter sp. C-17.不动杆菌属C-17菌株壳聚糖酶的发酵条件及性质
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8
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9
Lytic enzyme complex of an antagonistic Bacillus sp. X-b: isolation and purification of components.拮抗芽孢杆菌X-b的溶菌酶复合物:各组分的分离与纯化
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10
A novel chitinase having a unique mode of action from Aspergillus fumigatus YJ-407.一种来自烟曲霉YJ - 407的具有独特作用模式的新型几丁质酶。
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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.

DOI:10.1631/jzus.2007.B0831
PMID:17973345
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2064955/
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。