title: Screening and characterization of a thermostable lipase from marine Streptomyces sp. strain W007.
abstract: A screening method along with the combination of genome sequence of microorganism, pairwise alignment, and lipase classification was used to search the thermostable lipase. Then, a potential thermostable lipase (named MAS1) from marine Streptomyces sp. strain W007 was expressed in Pichia pastoris X-33, and the biochemical properties were characterized. Lipase MAS1 belongs to the subfamily I.7, and it has 38% identity to the well-characterized Bacillus subtilis thermostable lipases in the subfamily I.4. The purified enzyme was estimated to be 29 kDa. The enzyme showed optimal temperature at 40 °C, and retained more than 80% of initial activity after 1 H incubation at 60 °C, suggesting that MAS1 was a thermostable lipase. MAS1 was an alkaline enzyme with optimal pH value at 7.0 and had stable activity for 12 H of incubation at pH 6.0-9.0. It was stable and retained about 90% of initial activity in the presence of Cu(2+) , Ca(2+) , Ni(2+) , and Mg(2+) , whereas 89.05% of the initial activity was retained when ethylene diamine tetraacetic acid was added. MAS1 showed the tolerance to organic solvents, but was inhibited by various surfactants. MAS1 was verified to be a triglyceride lipase and could hydrolyze triacylglycerol and diacylglycerol. The result represents a good example for researchers to discover thermostable lipase for industrial application.
authors: College of Light Industry and Food Sciences, Key Lab of Fermentation and Enzyme Engineering, South China University of Technology, Guangzhou, People's Republic of China.
authors: Dongjuan
authors: D
authors: Yuan
authors: College of Light Industry and Food Sciences, Key Lab of Fermentation and Enzyme Engineering, South China University of Technology, Guangzhou, People's Republic of China.
authors: Dongming
authors: D
authors: Lan
authors: College of Light Industry and Food Sciences, Key Lab of Fermentation and Enzyme Engineering, South China University of Technology, Guangzhou, People's Republic of China.
authors: Ruipu
authors: R
authors: Xin
authors: School of Bioscience and Bioengineering, South China University of Technology, Guangzhou, People's Republic of China.
authors: Bo
authors: B
authors: Yang
authors: College of Light Industry and Food Sciences, Key Lab of Fermentation and Enzyme Engineering, South China University of Technology, Guangzhou, People's Republic of China.
authors: Yonghua
authors: Y
authors: Wang
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D003001:Cloning, Molecular; D004795:Enzyme Stability; D008049:Lipase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D010802:Phylogeny; D010843:Pichia / Q000235:genetics; D016415:Sequence Alignment; D013302:Streptomyces / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D008049:Lipase; C428386:thermostable lipase
keywords: Streptomyces sp. strain W007; pairwise alignment; thermostable lipase; triacylglycerol lipase