title: Cloning, Expression, and Characterization of a Cold-Adapted and Surfactant-Stable Alginate Lyase from Marine Bacterium Agarivorans sp. L11.
abstract: The purpose of this study was to find a cold-adapted and surfactant-stable alginate lyase as a candidate for biotechnological and industrial applications. The gene for a new alginate lyase, AlyL1, from Agarivorans sp. L11 was cloned and expressed in Escherichia coli. The recombinant AlyL1 was most active at 40°C (1,370 U/mg). It was a cold-adapted alginate lyase, which showed 54.5% and 72.1% of maximum activity at 15°C and 20°C, respectively. AlyL1 was an alkaliphilic enzyme and most active at pH 8.6. In addition, it showed high stability in the presence of various surfactants at a high concentration (from 0.1% to 1% (w/v)). AlyL1 was an endo-type alginate lyase that degraded both polyM and polyG blocks, yielding disaccharides and trisaccharides as the main products. This is the first report of the cloning and functional expression of a cold-adapted and surfactant-stable alginate lyase. AlyL1 might be an interesting candidate for biotechnological and industrial applications.
authors.affiliation: Key Laboratory of Marine Drugs, Chinese Ministry of Education; Shandong Provincial Key Laboratory of Glycoscience and Glycotechnology, School of Medicine and Pharmacy, Ocean University of China, Qingdao 266003, P.R. China.
authors.forename: Shangyong
authors.initials: S
authors.lastname: Li
authors.affiliation: Key Laboratory of Marine Drugs, Chinese Ministry of Education; Shandong Provincial Key Laboratory of Glycoscience and Glycotechnology, School of Medicine and Pharmacy, Ocean University of China, Qingdao 266003, P.R. China.
authors.forename: Xuemei
authors.initials: X
authors.lastname: Yang
authors.affiliation: Key Laboratory of Marine Drugs, Chinese Ministry of Education; Shandong Provincial Key Laboratory of Glycoscience and Glycotechnology, School of Medicine and Pharmacy, Ocean University of China, Qingdao 266003, P.R. China.
authors.forename: Lan
authors.initials: L
authors.lastname: Zhang
authors.affiliation: Key Laboratory of Marine Drugs, Chinese Ministry of Education; Shandong Provincial Key Laboratory of Glycoscience and Glycotechnology, School of Medicine and Pharmacy, Ocean University of China, Qingdao 266003, P.R. China.
authors.forename: Wengong
authors.initials: W
authors.lastname: Yu
authors.affiliation: Key Laboratory of Marine Drugs, Chinese Ministry of Education; Shandong Provincial Key Laboratory of Glycoscience and Glycotechnology, School of Medicine and Pharmacy, Ocean University of China, Qingdao 266003, P.R. China.
authors.forename: Feng
authors.initials: F
authors.lastname: Han
mesh_terms: D034241:Alteromonadaceae / Q000201:enzymology / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D003001:Cloning, Molecular; D003080:Cold Temperature; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D011133:Polysaccharide-Lyases / Q000737:chemistry* / Q000378:metabolism*; D015202:Protein Engineering; D013501:Surface-Active Agents
chemical_list: D001426:Bacterial Proteins; D013501:Surface-Active Agents; D011133:Polysaccharide-Lyases; C016158:poly(beta-D-mannuronate) lyase