标题:Family-level diversity of extracellular proteases of sedimentary bacteria from the South China Sea
作者:Yang J.; Feng Y.; Chen X.; Xie B.; Zhang Y.; Shi M.; Zhang X.
作者机构:[Yang, J] State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Qingdao, 266237, China, Institute o 更多
通讯作者:Zhang, X(zhangxiying@sdu.edu.cn)
通讯作者地址:[Zhang, X] State Key Laboratory of Microbial Technology, Marine Biotechnology Research Center, Shandong UniversityChina;
来源:Acta Oceanologica Sinica
出版年:2019
DOI:10.1007/s13131-019-1391-9
关键词:diversity; extracellular proteases; N-terminal amino acid sequencing; protease families; protease-producing bacteria; South China Sea
摘要:Protease-producing bacteria and their extracellular proteases are key players in degrading organic nitrogen to drive marine nitrogen cycling and yet knowledge on both of them is still very limited. This study screened protease-producing bacteria from the South China Sea sediments and analyzed the diversity of their extracellular proteases at the family level through N-terminal amino acid sequencing. Results of the 16S rRNA gene sequence analysis showed that all screened protease-producing bacteria belonged to the class Gammaproteobacteria and most of them were affiliated with different genera within the orders Alteromonadales and Vibrionales. The Nterminal amino acid sequence analysis for fourteen extracellular proteases from fourteen screened bacterial strains revealed that all these proteases belonged to the M4 family of metalloproteases or the S8 family of serine proteases. This study presents new details on taxa of marine sedimentary protease-producing bacteria and types of their extracellular proteases, which will help to comprehensively understand the process and mechanism of the microbial enzymatic degradation of marine sedimentary organic nitrogen. © 2019, Chinese Society for Oceanography and Springer-Verlag GmbH Germany, part of Springer Nature.
收录类别:SCOPUS
资源类型:期刊论文
原文链接:https://www.scopus.com/inward/record.uri?eid=2-s2.0-85067644776&doi=10.1007%2fs13131-019-1391-9&partnerID=40&md5=22244394a78111b1bc30f4c3f8a3c88f
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