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Expression and Characterization of a Novel Thermo-Alkalistable Lipase from Hyperthermophilic Bacterium Thermotoga maritima
Tian, Rui1; Chen, Huayou1,2,3; Ni, Zhong1; Zhang, Qing1; Zhang, Zhongge3; Zhang, Tianxi1; Zhang, Chunxia1; Yang, Shengli1
2015-07-01
Source PublicationAPPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
ISSN0273-2289
Volume176Issue:5Pages:1482-1497
Abstract

A gene coding for lipase (Tm1350) from the hyperthermophilic bacterium Thermotoga maritima MSB8 was cloned and overexpressed by Escherichia coli. The enzyme can degrade substrates with both short and long acyl chain lengths. The apparent Km and Vmax values for p-nitrophenyl butyrate were 8 mM and 333 U/mg, respectively. The enzyme displayed optimal activity at pH 7.5 and 70 A degrees C, maintained 66 % of the original activity after 8 h of incubation, and its half-lives at pHs 9 and 10 were 8 and 1 h. The activity of Tm1350 was stimulated up to 131 or 151 % of the original activity by incubating with 4 M urea or 20 % (v/v) methanol, and 90.1 or 70.2 % of the activity was maintained after 8 h incubation of the enzyme in 20 or 75 % (v/v) of the methanol, showing potential for biodiesel production. The activity of the enzyme without cysteine residue was stimulated up to 618 and 550 % of the original activity by incubating with dithiothreitol (DTT) and reduced glutathione (GSH) at a concentration of 1 mM. However, the circular dichroism spectra of the enzyme have no obvious change after DTT treatment. It is speculated that DTT interacts with potential residues in some key active sites without influence of structure.

KeywordLipase Thermostable Enzyme Thermotoga Maritima Alkali Resistance Methanol-activated
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
DOI10.1007/s12010-015-1659-2
Indexed BySCI
Language英语
WOS KeywordHIGH-LEVEL EXPRESSION ; PYROCOCCUS-FURIOSUS ; ORGANIC-SOLVENTS ; PURIFICATION ; ESTERASE ; STRAIN ; ENZYME ; LYSOPHOSPHOLIPASE ; DITHIOTHREITOL ; REAGENT
WOS Research AreaBiochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
WOS SubjectBiochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
WOS IDWOS:000358379400018
Citation statistics
Cited Times:2[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/19412
Collection生化工程国家重点实验室
Affiliation1.Jiangsu Univ, Inst Life Sci, Zhenjiang 212013, Peoples R China
2.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 10090, Peoples R China
3.Univ Calif San Diego, Div Biol Sci, La Jolla, CA 92093 USA
Recommended Citation
GB/T 7714
Tian, Rui,Chen, Huayou,Ni, Zhong,et al. Expression and Characterization of a Novel Thermo-Alkalistable Lipase from Hyperthermophilic Bacterium Thermotoga maritima[J]. APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY,2015,176(5):1482-1497.
APA Tian, Rui.,Chen, Huayou.,Ni, Zhong.,Zhang, Qing.,Zhang, Zhongge.,...&Yang, Shengli.(2015).Expression and Characterization of a Novel Thermo-Alkalistable Lipase from Hyperthermophilic Bacterium Thermotoga maritima.APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY,176(5),1482-1497.
MLA Tian, Rui,et al."Expression and Characterization of a Novel Thermo-Alkalistable Lipase from Hyperthermophilic Bacterium Thermotoga maritima".APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY 176.5(2015):1482-1497.
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