Production and Characterization of Enzymes Involved in Chitin Catabolic Cascade from a Bacterial Strain Isolated from Soil

Ji Hyun Lee, J. Lee, So Yeon Park, Yoo-kyeong Jang, Y. Lim, Hye Yoon Lee, Young Min Jung, Hae Chang Lee, Jong Hwa Lee, S. Amna, Jae Kweon Park
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引用次数: 1

Abstract

The present study was aimed to isolate the bacteria producing chitinolytic enzymes including chitin deacetylase (CDA) from soil origin. About 24 bacteria were screened for their chitinolytic enzymes producing ability on the basis of colloidal chitin. Amongst one of the most potent isolates designated to JI-02 was further selected as the most prominent chitinolytic and CDAlike enzyme (CDA-X) producer based on the ability of deacetylation of an artificial substrate pNP-acetamilide. The maximum production of CDA-X in crude enzyme from JI-02 was observed in the presence of 1% colloidal chitin at 37°C and pH 6.4 after 120 h of incubation. Potent enzyme activity of CDA-X was determined toward pNP-acetamilide, demonstrating that optimal pH, temperature and ionic strength of the CDA-X were assessed to be 7.0, 52°C and 125 mM, respectively. Unexpectedly, Nacetylglucosamine (GlcNAc) was not fully converted by the action of CDA-X to glucosamine (GlcN) under the established conditions. Further study on enzyme activity toward chitin-oligosaccharides consisting of multi-N-acetylglucosamine (GlcNAc)n, n=2-5 may be necessary to elucidate the mode of action which requires the minimum size of (GlcNAc)n. However, our data suggest that CDA-X can convert chitin to chitosan with the maximum yield of approximately 0.08g/L during the fermentation of the strain in the presence of chitin. Furthermore, we found that crude enzyme showed the significant chitosanolytic activity. Taken together, our data suggest that the strain JI-02 may be a potential candidate as a particular strain for better understating of chitin catabolic pathway.
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一株土壤细菌甲壳素分解代谢级联酶的产生及特性研究
本研究旨在从土壤中分离产生几丁质降解酶的细菌,包括几丁质脱乙酰酶(CDA)。筛选了24种以胶体几丁质为基础产生几丁质水解酶的细菌。其中一个最有效的分离株被指定为JI-02,进一步被选为最突出的几丁质水解和CDAlike酶(CDA-X)的生产者,基于人工底物pnp -乙酰酰胺的去乙酰化能力。在37℃、pH 6.4、胶体甲壳素含量为1%的条件下,JI-02粗酶在培养120 h后,da - x的产量最大。测定了CDA-X对pNP-acetamilide的有效酶活性,表明CDA-X的最佳pH、温度和离子强度分别为7.0℃、52℃和125 mM。出乎意料的是,在既定条件下,Nacetylglucosamine (GlcNAc)并没有被CDA-X完全转化为glucosamine (GlcN)。进一步研究酶对多n-乙酰氨基葡萄糖(GlcNAc)n, n=2-5组成的几丁质寡糖的活性,可能有必要阐明需要最小尺寸(GlcNAc)n的作用方式。然而,我们的数据表明,在甲壳素存在的菌株发酵过程中,CDA-X可以将甲壳素转化为壳聚糖,最高产量约为0.08g/L。此外,我们发现粗酶具有显著的壳聚糖水解活性。综上所述,我们的数据表明菌株JI-02可能是一个潜在的候选菌株,可以更好地理解几丁质分解代谢途径。
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