干旱区生态环境知识资源中心(Arid): Cloning, Characterization, and Structural Modeling of an Extremophilic Bacterial Lipase Isolated from Saline Habitats of the Thar Desert

Arid

DOI	10.1007/s12010-020-03329-3
	Cloning, Characterization, and Structural Modeling of an Extremophilic Bacterial Lipase Isolated from Saline Habitats of the Thar Desert
	Verma, Swati 1; Kumar, Rajender 2; Kumar, Pradeep 3; Sharma, Deepak 3; Gahlot, Hukam 4; Sharma, Pushpender Kumar 5; Meghwanshi, Gautam Kumar 1
通讯作者	Meghwanshi, Gautam Kumar
来源期刊	APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
ISSN	0273-2289
EISSN	1559-0291
出版年	2020
卷号	192 期号:2 页码:557-572
英文摘要	Lipases have a characteristic folding pattern of alpha/beta-hydrolase with mostly parallel beta-sheets, flanked on both sides by alpha-helixes in the structure. The active site is formed by a catalytic triad (serine, aspartic/glutamic acid, and histidine), which is highly conserved. In this study, we have used an integrated experimental and computational approach to identify the extremophilic microbial lipases from the saline habitats of the Thar Desert of Rajasthan. Lipase-producing bacteria were screened and a few samples showed significant lipase activity in both quantitative and qualitative experiments. 16S rRNA sequence analysis of the isolate F1 showed that its sequence is quite similar to that of Bacillus licheniformis and Bacillus haynesii, indicating that this isolate belongs to a new subspecies of Bacillus. The isolate F7 showed maximum sequence identity with Bacillus tequilensis strain 10b. The isolate F7 sequence analysis provided a clear testimony that it can be a new strain of Bacillus tequilensis. The F7 lipase exhibited optimal activity at 60 degrees C and pH 9. Structural modeling of the F7 lipase revealed that it has a highly conserved alpha/beta hydrolase fold at the sequence and structural level except for the N-terminal region. Interestingly, residue Glu128 was different from the template structure and showed the hydrogen bonding between the side chain of Glu128 and side chains of Asn35 and Gln152 amino acids. Besides, this amino acid also showed salt bridge interaction between Glu128--Lys101. These interactions may be assisting in preserving the stability and activity of lipase at high temperatures and in alkaline pH conditions. The information gathered from this investigation will guide in the rational designing of new more potential extremophilic lipase.
英文关键词	Lipases Extremophilic Thar Desert Arid regions Bacillus tequilensis Molecular modeling Signal peptide Thermoalkaliphilic
类型	Article
语种	英语
国家	India ; Sweden
收录类别	SCI-E
WOS记录号	WOS:000534287500002
WOS关键词	EXTRACELLULAR LIPASE ; BACILLUS ; PURIFICATION ; METAGENOME ; INSIGHTS ; ENZYMES ; STRAIN
WOS类目	Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
WOS研究方向	Biochemistry & Molecular Biology ; Biotechnology & Applied Microbiology
资源类型	期刊论文
条目标识符	http://119.78.100.177/qdio/handle/2XILL650/319135
作者单位	1.Maharaja Ganga Singh Univ, Dept Microbiol, Bikaner 334004, India; 2.Umea Univ, Dept Clin Microbiol, SE-90185 Umea, Sweden; 3.CSIR Inst Microbial Technol, GNRPC, Chandigarh 160036, India; 4.JN Vyas Univ, Dept Bot, Microbial Genom Lab, Jodhpur 342001, Rajasthan, India; 5.Sri Guru Granth Sahib World Univ, Dept Biotechnol, Fatehgarh Sahib, Punjab, India
推荐引用方式 GB/T 7714	Verma, Swati,Kumar, Rajender,Kumar, Pradeep,et al. Cloning, Characterization, and Structural Modeling of an Extremophilic Bacterial Lipase Isolated from Saline Habitats of the Thar Desert[J],2020,192(2):557-572.
APA	Verma, Swati.,Kumar, Rajender.,Kumar, Pradeep.,Sharma, Deepak.,Gahlot, Hukam.,...&Meghwanshi, Gautam Kumar.(2020).Cloning, Characterization, and Structural Modeling of an Extremophilic Bacterial Lipase Isolated from Saline Habitats of the Thar Desert.APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY,192(2),557-572.
MLA	Verma, Swati,et al."Cloning, Characterization, and Structural Modeling of an Extremophilic Bacterial Lipase Isolated from Saline Habitats of the Thar Desert".APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY 192.2(2020):557-572.