{"title":"苍山节杆菌CSAJ-16中性尿囊的克隆、异源表达及鉴定。","authors":"Xin Yan, Wei Hu, Yun-Guo Zhu, Qing-Qing Liu, Shuai Wang, Hong-Yan Liu, Dan Zhu, Zhi-Hua Lv, Lin-Hua Li, Yi-Rui Yin","doi":"10.33073/pjm-2023-027","DOIUrl":null,"url":null,"abstract":"<p><p>Uricase (or Urate oxidase), a key enzyme involved in purine metabolism, is commonly used in treating conditions such as gout, hyperuricemia, and tumor lysis syndrome. In this study, a uricase-producing strain (named CSAJ-16) was isolated from the soil sample of Cangshan Mountain, Yunnan Province, China. This strain was identified as <i>Arthrobacter</i> sp. CSAJ-16. Based on the gene sequence alignment, the uricase gene (named <i>aruox</i>) of <i>Arthrobacter</i> sp. CSAJ-16 was amplified and heterologously expressed. The recombinant uricase (ArUOX) was about 32 kDa. The optimal pH and temperature of ArUOX were pH 7 and 20°C, respectively. The ArUOX remained above 50% relative activity after incubation at 37°C for 100 min or at pH 6.0-8.6 for 24 h. Moreover, metal ions such as K<sup>+</sup>, Mg<sup>2+</sup>, Ca<sup>2+</sup>, Ba<sup>2+</sup> and Pb<sup>2+</sup> can significantly enhance the activity of ArUOX (> 200%). These enzymatic properties indicate that ArUOX has potential applications in pharmaceutical enzymes and uric acid detection kits.</p>","PeriodicalId":94173,"journal":{"name":"Polish journal of microbiology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2023-09-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/4e/f1/pjm-72-3-pjm-2023-027.PMC10561068.pdf","citationCount":"0","resultStr":"{\"title\":\"Cloning, Heterologous Expression, and Characterization of a Neutral Uricase from <i>Arthrobacter</i> sp. CSAJ-16 in Cangshan Mountain.\",\"authors\":\"Xin Yan, Wei Hu, Yun-Guo Zhu, Qing-Qing Liu, Shuai Wang, Hong-Yan Liu, Dan Zhu, Zhi-Hua Lv, Lin-Hua Li, Yi-Rui Yin\",\"doi\":\"10.33073/pjm-2023-027\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Uricase (or Urate oxidase), a key enzyme involved in purine metabolism, is commonly used in treating conditions such as gout, hyperuricemia, and tumor lysis syndrome. In this study, a uricase-producing strain (named CSAJ-16) was isolated from the soil sample of Cangshan Mountain, Yunnan Province, China. This strain was identified as <i>Arthrobacter</i> sp. CSAJ-16. Based on the gene sequence alignment, the uricase gene (named <i>aruox</i>) of <i>Arthrobacter</i> sp. CSAJ-16 was amplified and heterologously expressed. The recombinant uricase (ArUOX) was about 32 kDa. The optimal pH and temperature of ArUOX were pH 7 and 20°C, respectively. The ArUOX remained above 50% relative activity after incubation at 37°C for 100 min or at pH 6.0-8.6 for 24 h. Moreover, metal ions such as K<sup>+</sup>, Mg<sup>2+</sup>, Ca<sup>2+</sup>, Ba<sup>2+</sup> and Pb<sup>2+</sup> can significantly enhance the activity of ArUOX (> 200%). These enzymatic properties indicate that ArUOX has potential applications in pharmaceutical enzymes and uric acid detection kits.</p>\",\"PeriodicalId\":94173,\"journal\":{\"name\":\"Polish journal of microbiology\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2023-09-20\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/4e/f1/pjm-72-3-pjm-2023-027.PMC10561068.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Polish journal of microbiology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.33073/pjm-2023-027\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2023/9/1 0:00:00\",\"PubModel\":\"eCollection\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Polish journal of microbiology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.33073/pjm-2023-027","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2023/9/1 0:00:00","PubModel":"eCollection","JCR":"","JCRName":"","Score":null,"Total":0}
Cloning, Heterologous Expression, and Characterization of a Neutral Uricase from Arthrobacter sp. CSAJ-16 in Cangshan Mountain.
Uricase (or Urate oxidase), a key enzyme involved in purine metabolism, is commonly used in treating conditions such as gout, hyperuricemia, and tumor lysis syndrome. In this study, a uricase-producing strain (named CSAJ-16) was isolated from the soil sample of Cangshan Mountain, Yunnan Province, China. This strain was identified as Arthrobacter sp. CSAJ-16. Based on the gene sequence alignment, the uricase gene (named aruox) of Arthrobacter sp. CSAJ-16 was amplified and heterologously expressed. The recombinant uricase (ArUOX) was about 32 kDa. The optimal pH and temperature of ArUOX were pH 7 and 20°C, respectively. The ArUOX remained above 50% relative activity after incubation at 37°C for 100 min or at pH 6.0-8.6 for 24 h. Moreover, metal ions such as K+, Mg2+, Ca2+, Ba2+ and Pb2+ can significantly enhance the activity of ArUOX (> 200%). These enzymatic properties indicate that ArUOX has potential applications in pharmaceutical enzymes and uric acid detection kits.