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一株产透明质酸酶的菌株鉴定及酶学性质研究

Identification of a Hyaluronidase Producing Strain and Study on Its Enzymatic Properties
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摘要 透明质酸酶可用于药物渗透剂、动物皮革松散及低分子量的透明质酸制备。实验室前期筛选了一株具有较高透明质酸降解能力的菌株,本研究对其进行了16S rRNA基因和生理生化反应鉴定,鉴定为弗氏柠檬酸杆菌,但弗氏柠檬酸杆菌来源的透明质酸酶的功能还未见报道。因而,以透明质酸为底物研究其酶学性质,结果表明:该酶最适pH值为5.5,在pH值4.0~8.0下处理1 h可以保持60%以上酶活力;最适温度为50℃,在50℃和60℃下处理1 h后剩余60%以上的酶活力。该酶和人源透明质酸酶最适pH相似,但其耐热性更高。因此,本研究挖掘到了新颖的透明质酸酶的资源,并为其开发利用提供了参考价值。 Hyaluronidase can be used in pharmaceutical penetrants, animal leather loose and the preparation of low molecular weight hyaluronic acid. A strain with high hyaluronic acid degradation ability was early screened in the laboratory. In this study, the strain was identified by the 16 S rRNA gene and biochemical reactions analysis.The result revealed that it was Citrobacter freundii. However, the function of the hyaluronidase from C. freundii had not yet been reported. Therefore, hyaluronic acid was used as substrate to study the enzyme properties. The results showed that the optimum pH was 5.5, and the enzyme activity was maintained above 60% after treatment at pH 4.0~8.0 for 1 h;the optimum temperature was 50 ℃, and the enzyme activity was remained more than 60% after treatment at 50 ℃ and 60 ℃ for 1 h. The optimum pH of the enzyme from C. freundii was similar to that of human hyaluronidase, but the heat resistance was higher. This study explored a novel hyaluronidase resource and provided a reference value for its future.
作者 雷曦 周峻沛 黄遵锡 岑潇龙 杨露 张蕊 Lei Xi;Zhou Junpei;Huang Zunxi;Cen Xiaolong;Yang Lu;Zhang Rui(School of Life Science,Yunnan Nonnal University,Kunming,650500;Engineering Research Center of Ministry of Education for Sustainable Development and Utilization of Biomass Energy,Key Laboratory of Yunnan for Biomass Energy and Biotechnology of Environment,Key Laboratory of Enzyme Engineering,Yunnan Normal University,Kunming,650500)
出处 《基因组学与应用生物学》 CAS CSCD 北大核心 2021年第4期1604-1610,共7页 Genomics and Applied Biology
基金 国家重点研发计划项目(2017YFB0308401) 国家自然科学基金项目(31460694)共同资助。
关键词 透明质酸酶 菌株鉴定 酶学性质 Hyaluronidase Bacterial identification Enzymatic properties
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