title: Biochemical properties of a new cold-active mono- and diacylglycerol lipase from marine member Janibacter sp. strain HTCC2649.
abstract: Mono- and di-acylglycerol lipase has been applied to industrial usage in oil modification for its special substrate selectivity. Until now, the reported mono- and di-acylglycerol lipases from microorganism are limited, and there is no report on the mono- and di-acylglycerol lipase from bacteria. A predicted lipase (named MAJ1) from marine Janibacter sp. strain HTCC2649 was purified and biochemical characterized. MAJ1 was clustered in the family I.7 of esterase/lipase. The optimum activity of the purified MAJ1 occurred at pH 7.0 and 30 °C. The enzyme retained 50% of the optimum activity at 5 °C, indicating that MAJ1 is a cold-active lipase. The enzyme activity was stable in the presence of various metal ions, and inhibited in EDTA. MAJ1 was resistant to detergents. MAJ1 preferentially hydrolyzed mono- and di-acylglycerols, but did not show activity to triacylglycerols of camellia oil substrates. Further, MAJ1 is low homologous to that of the reported fungal diacylglycerol lipases, including Malassezia globosa lipase 1 (SMG1), Penicillium camembertii lipase U-150 (PCL), and Aspergillus oryzae lipase (AOL). Thus, we identified a novel cold-active bacterial lipase with a sn-1/3 preference towards mono- and di-acylglycerides for the first time. Moreover, it has the potential, in oil modification, for special substrate selectivity.
authors.affiliation: College of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510640, China. dongjuanyuan@gmail.com.
authors.forename: Dongjuan
authors.initials: D
authors.lastname: Yuan
authors.affiliation: College of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510640, China. dmlan@scut.edu.cn.
authors.forename: Dongming
authors.initials: D
authors.lastname: Lan
authors.affiliation: College of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510640, China. catherinexin0116@sina.com.
authors.forename: Ruipu
authors.initials: R
authors.lastname: Xin
authors.affiliation: School of Bioscience and Bioengineering, South China University of Technology, Guangzhou 510006, China. yangbo@scut.edu.cn.
authors.forename: Bo
authors.initials: B
authors.lastname: Yang
authors.affiliation: College of Light Industry and Food Sciences, South China University of Technology, Guangzhou 510640, China. yonghw@scut.edu.cn.
authors.forename: Yonghua
authors.initials: Y
authors.lastname: Wang
mesh_terms: D000192:Actinomycetales / Q000145:classification / Q000201:enzymology*; D000595:Amino Acid Sequence; D001230:Aspergillus / Q000145:classification / Q000201:enzymology; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008071:Lipoprotein Lipase / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D008994:Monoacylglycerol Lipases / Q000737:chemistry / Q000378:metabolism*; D010407:Penicillium / Q000145:classification / Q000201:enzymology; D010802:Phylogeny; D055550:Protein Stability; D016415:Sequence Alignment; D012997:Solvents / Q000737:chemistry; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D005656:Fungal Proteins; D012997:Solvents; D008994:Monoacylglycerol Lipases; D008071:Lipoprotein Lipase