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Impact of orientation and flexibility of peptide linkers on T-maritima lipase Tm1350 displayed on Bacillus subtilis spores surface using CotB as fusion partner
Ullah, Jawad1; Chen, Huayou1,2; Vastermark, Ake3,4; Jia, Jinru1; Wu, Bangguo1; Ni, Zhong1; Le, Yilin1; Wang, Hongcheng1
2017-09-01
Source PublicationWORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY
ISSN0959-3993
Volume33Issue:9Pages:166
Abstract

Fusion protein construction often requires peptide linkers for prolonged conformation, extended stability and enzyme activity. In this study a series of fusion between Thermotoga maritima lipase Tm1350 and Bacillus subtillis coat protein CotB, comprising of several peptide linkers, with different length, flexibility and orientations were constructed. Effects of temperature, pH and chemicals were examined, on the activity of displayed enzyme. The fusion protein with longer flexible linkers L9 [(GGGGS)(4)] and L7 (GGGGS-GGGGS-EAAAK-EAAAK-GGGGS-GGGGS) possess 1.29 and 1.16-fold higher activity than the original, under optimum temperature and pH respectively. Moreover, spore surface displaying Tm1350 with L3 (EAAAK-GGGGS) and L9 ((GGGGS) 4) showed extended thermostably, maintaining 1.40 and 1.35-fold higher activity than the original respectively, at 80 degrees C after 5 h of incubation. The enzyme activity of linkers with different orientation, including L5, L6 and L7 was determined, where L7 maintained 1.05 and 1.27-fold higher activity than L5 and L6. Effect of 0.1% proteinase K, bromelain, 20% ethanol and 30% methanol was investigated. Linkers with appropriate Glycine residues (flexible) showed higher activity than Alanine residues (rigid). The activity of the displayed enzyme can be improved by maintaining orientation and flexibility of peptide linkers, to evaluate high activity and stability in industrial processes.

KeywordBacillus Subtilis Enzyme Activity Linkers Surface Display Tm1350
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
DOI10.1007/s11274-017-2327-1
Indexed BySCI
Language英语
WOS KeywordDOMAIN LINKERS ; ANCHOR PROTEIN ; MSB8 NITRILASE ; COAT ; ACTIVATION ; CARRIER ; ENZYME ; DESIGN ; SYSTEM
WOS Research AreaBiotechnology & Applied Microbiology
WOS SubjectBiotechnology & Applied Microbiology
Funding OrganizationOpen Funding Project of National Key Laboratory of Biochemical Engineering, The Key R&D Program of Jiangsu Province (Modern Agriculture), China(BE2017355) ; Open Funding Project of the State Key Laboratory of Bioreactor Engineering ; Agricultural Sci-Tech Self-Innovation Program of Jiangsu Province, China(CX(17)3044) ; JSPS fellowship(PE 16042)
WOS IDWOS:000411062900005
Citation statistics
Cited Times:1[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/23228
Collection生化工程国家重点实验室
Affiliation1.Jiangsu Univ, Inst Life Sci, Zhenjiang 212000, Jiangsu, Peoples R China
2.Chinese Acad Sci, Inst Proc Engn, Natl Key Lab Biochem Engn, Beijing 100190, Peoples R China
3.Univ Calif San Diego, Div Biol Sci, La Jolla, CA 92093 USA
4.Nitech, Showa Ku, Nagoya, Aichi 4668555, Japan
Recommended Citation
GB/T 7714
Ullah, Jawad,Chen, Huayou,Vastermark, Ake,et al. Impact of orientation and flexibility of peptide linkers on T-maritima lipase Tm1350 displayed on Bacillus subtilis spores surface using CotB as fusion partner[J]. WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY,2017,33(9):166.
APA Ullah, Jawad.,Chen, Huayou.,Vastermark, Ake.,Jia, Jinru.,Wu, Bangguo.,...&Wang, Hongcheng.(2017).Impact of orientation and flexibility of peptide linkers on T-maritima lipase Tm1350 displayed on Bacillus subtilis spores surface using CotB as fusion partner.WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY,33(9),166.
MLA Ullah, Jawad,et al."Impact of orientation and flexibility of peptide linkers on T-maritima lipase Tm1350 displayed on Bacillus subtilis spores surface using CotB as fusion partner".WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY 33.9(2017):166.
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