Expression and characterization of a bifunctional alginate lyase named Al163 from the Antarctic bacterium Pseudoalteromonas sp. NJ-21

	Expression and characterization of a bifunctional alginate lyase named Al163 from the Antarctic bacterium Pseudoalteromonas sp. NJ-21
	Xie Maisheng 1; Li Jiang 2; He Peiqing 2; Lin Xuezheng 2
刊名	Journal of Oceanology and Limnology
	2018
卷号	36 期号:4 页码:1304-1314
关键词	Pseudoalteromonas sp. alginate lyase PL-6 family
ISSN号	2096-5508
英文摘要	In this study, an endolytic alginate lyase, named Al163, was identified, cloned, and characterized from the Antarctic bacterium Pseudoalteromonas sp. NJ-21. Comparative sequence analysis showed that the predicted amino acid sequence encoded by al163 belongs to the polysaccharide lyase 6(PL-6) family and has a molecular mass of about 80 kDa. Recombinant enzyme was purified by Ni-Sepharose affinity chromatography. Recombinant Al163 exhibited maximum activity(258 U/mg) at pH 7.0 and 40 ° C, and thermal stability assays showed retention of almost 90% activity after incubation at 30 ° C for 30 min. Al163 activity was stimulated by Cd~(2+) , Ca~(2+) , Fe~(3+) , and Mn~(2+) , but inhibited by Cu~(2+) , Si~(2+) , Fe~(2+) , and Ni~(2+) . Thin-layer chromatographic analysis indicated that Al163 degraded sodium alginate, polyM, and polyG, generating disaccharides and trisaccharides as the final products. Only a few bacterial strains that produce a bifunctional alginate lyase have been reported. Our results indicate that recombinant Al163 exhibits broad substrate specificity and its products exhibit low degrees of polymerization. Both properties imply high potential for use of the enzyme in several industrial fields, including cosmetics and pharmaceuticals, based on the high demand for biologically active oligosaccharides.
资助项目	Supported by the Public Science and Technology Research Funds Project of Ocean ; the Chinese Polar Environment Comprehensive Investigation & Assessment Programs ; the Basic Scientific Research Funds of First Institute of Oceanography, State Oceanic Administration (SOA) ; the Qingdao Applied Basic Research Project
WOS研究方向	Microbiology
语种	英语
CSCD记录号	CSCD:6315922
内容类型	期刊论文
源URL	[http://ir.fio.com.cn:8080/handle/2SI8HI0U/28861]
专题	自然资源部第一海洋研究所
作者单位	1.The First Institute of Oceanography,State Oceanic Administration (SOA), Key Laboratory of Marine Bioactive Substances,State Oceanic Administration (SOA), Qingdao, Shandong 266061, China 2.The First Institute of Oceanography,State Oceanic Administration (SOA);;Key Laboratory of Marine Natural Products of Qingdao, Key Laboratory of Marine Bioactive Substances,State Oceanic Administration (SOA);;Key Laboratory of Marine Natural Products of Qingdao, Qingdao;;Qingdao, ;; 266061;;266061 3.The First Institute of Oceanography,State Oceanic Administration (SOA);;Key Laboratory of Marine Natural Products of Qingdao, Key Laboratory of Marine Bioactive Substances,State Oceanic Administration (SOA);;Key Laboratory of Marine Natural Products of Qingdao, Qingdao;;Qingdao, ;; 266061;;266061 4.The First Institute of Oceanography,State Oceanic Administration (SOA);;Key Laboratory of Marine Natural Products of Qingdao, Key Laboratory of Marine Bioactive Substances,State Oceanic Administration (SOA);;Key Laboratory of Marine Natural Products of Qingdao, Qingdao;;Qingdao, ;; 266061;;266061
推荐引用方式 GB/T 7714	Xie Maisheng,Li Jiang,He Peiqing,et al. Expression and characterization of a bifunctional alginate lyase named Al163 from the Antarctic bacterium Pseudoalteromonas sp. NJ-21[J]. Journal of Oceanology and Limnology,2018,36(4):1304-1314.
APA	Xie Maisheng,Li Jiang,He Peiqing,&Lin Xuezheng.(2018).Expression and characterization of a bifunctional alginate lyase named Al163 from the Antarctic bacterium Pseudoalteromonas sp. NJ-21.Journal of Oceanology and Limnology,36(4),1304-1314.
MLA	Xie Maisheng,et al."Expression and characterization of a bifunctional alginate lyase named Al163 from the Antarctic bacterium Pseudoalteromonas sp. NJ-21".Journal of Oceanology and Limnology 36.4(2018):1304-1314.