Identification and Characterization of a Novel Thermophilic, Organic Solvent Stable Lipase of Bacillus from a Hot Spring

doi:10.1007/s11745-017-4265-y

	Identification and Characterization of a Novel Thermophilic, Organic Solvent Stable Lipase of Bacillus from a Hot Spring
	Li, Jiang 1,2; Liu, Xiumeng 1,2
刊名	LIPIDS
	2017-07
卷号	52 期号:7 页码:619-627
关键词	Lipase Thermophile Bacillus sp. Identification Characterization
ISSN号	0024-4201
DOI	10.1007/s11745-017-4265-y
英文摘要	A novel lipase gene lip256 was cloned and identified from the genomic library of hot spring strain Bacillus sp. HT19. The deduced amino acid sequence of lip256 has less than 32% identity to a predicted esterase (Cog1752) from Photobacterium leiognathi lrivu.4.1 and contains a novel motif (GTSAG) that differs from other clusters in the lipase superfamily. Following purification, a single band was obtained with a molecular mass of 33 kDa by SDS-PAGE, and the optimal temperature and pH for lipolytic activity of Lip25 were 70 A degrees C and 9.0, respectively. Lip256 exhibited high activity at high temperatures, with 40% maximum activity at 80 A degrees C and good stability at temperatures ranges between 50 and 80 A degrees C. Additionally, the enzyme was highly stable in the presence of butyl-alcohol, glycerol, acetonitrile, pyridine, and urea. However, the presence of acetone, methanol, trichloromethane, petroleum ether, hexane, tert-butanol, isopropanol, dithiothreitol, ethylenediaminetetraacetic acid, polyhexamethylene biguanide, dimethyl sulfoxide, benzene, Triton X-100, Tween-20, Tween-80, and sodium dodecyl sulfate suppressed or absolutely inhibited enzyme activity. Furthermore, Ca2+, Mg2+, and Cu2+ suppressed enzyme activity, whereas Na+, Fe3+, K+, Fe2+, and Sr2+ enhanced enzyme activity. The unique characteristics of novel lipase Lip256, including its thermo-alkaliphilic performance, high tolerance toward metal ions, inhibitors, and detergents, and high stability in organic solvents, implied that this enzyme might be an interesting candidate for industrial processes.
资助项目	key lab of marine bioactive substance and modern analytical technique, SOA[MBSMAT-2015-06]
WOS关键词	HORMONE-SENSITIVE LIPASE ; MICROBIAL LIPASES ; BIOCHEMICAL-PROPERTIES ; THERMOSTABLE LIPASE ; GENE CLONING ; PURIFICATION ; ESTERASES ; THERMOCATENULATUS ; CARBOXYLESTERASE ; OVEREXPRESSION
WOS研究方向	Biochemistry & Molecular Biology ; Nutrition & Dietetics
语种	英语
出版者	WILEY
WOS记录号	WOS:000404329000005
内容类型	期刊论文
源URL	[http://ir.fio.com.cn:8080/handle/2SI8HI0U/26751]
专题	自然资源部第一海洋研究所
通讯作者	Li, Jiang
作者单位	1.SOA, Inst Oceanog 1, Key Lab Marine Bioact Subst, Qingdao 266061, Peoples R China 2.Key Lab Marine Bioact Subst Qingdao, Qingdao 266061, Peoples R China
推荐引用方式 GB/T 7714	Li, Jiang,Liu, Xiumeng. Identification and Characterization of a Novel Thermophilic, Organic Solvent Stable Lipase of Bacillus from a Hot Spring[J]. LIPIDS,2017,52(7):619-627.
APA	Li, Jiang,&Liu, Xiumeng.(2017).Identification and Characterization of a Novel Thermophilic, Organic Solvent Stable Lipase of Bacillus from a Hot Spring.LIPIDS,52(7),619-627.
MLA	Li, Jiang,et al."Identification and Characterization of a Novel Thermophilic, Organic Solvent Stable Lipase of Bacillus from a Hot Spring".LIPIDS 52.7(2017):619-627.