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 Publication | APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
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ISSN | 0273-2289 |
Volume | 176Issue: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. |
Keyword | Lipase Thermostable Enzyme Thermotoga Maritima Alkali Resistance Methanol-activated |
Subtype | Article |
WOS Headings | Science & Technology ; Life Sciences & Biomedicine |
DOI | 10.1007/s12010-015-1659-2 |
Indexed By | SCI |
Language | 英语 |
WOS Keyword | HIGH-LEVEL EXPRESSION ; PYROCOCCUS-FURIOSUS ; ORGANIC-SOLVENTS ; PURIFICATION ; ESTERASE ; STRAIN ; ENZYME ; LYSOPHOSPHOLIPASE ; DITHIOTHREITOL ; REAGENT |
WOS Research Area | Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
WOS Subject | Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology |
WOS ID | WOS:000358379400018 |
Citation statistics | |
Document Type | 期刊论文 |
Identifier | http://ir.ipe.ac.cn/handle/122111/19412 |
Collection | 生化工程国家重点实验室 |
Affiliation | 1.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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Expression and Chara(951KB) | 期刊论文 | 出版稿 | 限制开放 | CC BY-NC-SA | Application Full Text |
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