Cloning and characterization of the first polysaccharide lyase family 6 oligoalginate lyase from marine Shewanella sp. Kz7

• Published in: Journal of biochemistry (Tokyo) Vol. 159; no. 1; pp. 77 - 86
• Main Authors: Li, Shangyong, Wang, Linna, Han, Feng, Gong, Qianhong, Yu, Wengong
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.01.2016
• Subjects: Alginates - metabolism; Amino Acid Sequence; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Biofuels; Biotechnology; Cloning, Molecular; Electrophoresis, Polyacrylamide Gel; Glucuronic Acid - metabolism; Hexuronic Acids - metabolism; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Poly G - metabolism; Polysaccharide-Lyases - chemistry; Polysaccharide-Lyases - genetics; Regular Papers; Seaweed - chemistry; Sequence Homology, Amino Acid; Shewanella - enzymology; Substrate Specificity; oligoalginate lyase; Shewanella sp. Kz7; PL family 6; PolyG block preferred; monosaccharide acid
• ISSN: 0021-924X; 1756-2651
• DOI: 10.1093/jb/mvv076

Alginate, the most abundant carbohydrate in brown macroalgae, is widely used in the food and pharmaceutical industries. Recently, alginate has attracted increasing attention, as it may serve as an alternative biomass for the production of biofuel. The degradation of alginate into monomeric units is the prerequisite for bioethanol production. All known oligoalginate lyases belong to the polysaccharide lyase (PL) family 7, 14, 15 and 17, and most of them preferred to degrade the polyM blocks to yield 4-deoxy-l-erythro-5-hexoseulose uronic acid as the primary product. In this study, we cloned an oligoalginate lyase gene, oalS6, from Shewanella sp. Kz7 and expressed it in Escherichia coli. The PL family 6 oligoalginate lyase (OalS6) has no significant sequence similarity with other known oligoalginate lyases. OalS6 contains a chondroitinase-like domain and was assigned to the PL family 6. This lyase is an exo-type oligoalginate lyase and prefer to depolymerize polyG block into 2, 4, 5, 6-tetrahydroxytetrahydro-2H-pyran-2-carboxylic acid. All of these results indicate that OalS6 is a novel oligoalginate lyase that is structurally and functionally different from other known oligoalginate lyases. This finding provides new insights into the development of biofuel processing biotechnologies from seaweed.