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Bacterial cell-surface displaying of thermo-tolerant glutamate dehydrogenase and its application in L-glutamate assay
Song, Jianxia1,2,3,4; Liang, Bo3,4; Han, Dongfei3,4; Tang, Xiangjiang3,4; Lang, Qiaolin3,4; Feng, Ruirui1,2; Han, Lihui1,2; Liu, Aihua3,4
2015-03-01
Source PublicationENZYME AND MICROBIAL TECHNOLOGY
Volume70Issue:1Pages:72-78
Abstract

In this paper, glutamate dehydrogenase (Gldh) is reported to efficiently display on Escherichia coli cell surface by using N-terminal region of ice the nucleation protein as an anchoring motif. The presence of Gldh was confirmed by SDS-PAGE and enzyme activity assay. Gldh was detected mainly in the outer membrane fraction, suggesting that the Gldh was displayed on the bacterial cell surface. The optimal temperature and pH for the bacteria cell-surface displayed Gldh (bacteria-Gldh) were 70 degrees C and 9.0, respectively. Additionally, the fusion protein retained almost 100% of its initial enzymatic activity after 1 month incubation at 4 degrees C. Transition metal ions could inhibit the enzyme activity to different extents, while common anions had little adverse effect on enzyme activity. Importantly, the displayed Gldh is most specific to L-glutamate reported so far. The bacterial Gldh was enabled to catalyze oxidization of L-glutamate with NADP(+) as cofactor, and the resultant NADPH can be detected spectrometrically at 340 nm. The bacterial-Gldh based L-glutamate assay was established, where the absorbance at 340 nm increased linearly with the increasing L-glutamate concentration within the range of 10-400 mu M. Further, the proposed approach was successfully applied to measure L-glutamate in real samples. (C) 2014 Elsevier Inc. All rights reserved.

SubtypeArticle
KeywordBacterial Surface Display L-glutamate Thermo-tolerant Glutamate Dehydrogenase Enzyme Inhibition L-glutamate Detection
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
DOI10.1016/j.enzmictec.2014.12.002
WOS KeywordICE-NUCLEATION PROTEIN ; ESCHERICHIA-COLI ; WHOLE-CELL ; GLUCOSE-DEHYDROGENASE ; ANCHORING MOTIF ; D-XYLOSE ; ORGANOPHOSPHORUS HYDROLASE ; CEREBROSPINAL-FLUID ; MODIFIED-ELECTRODE ; ORGANIC-SOLVENTS
Indexed BySCI
Language英语
WOS Research AreaBiotechnology & Applied Microbiology
WOS SubjectBiotechnology & Applied Microbiology
WOS IDWOS:000350094500010
Citation statistics
Cited Times:11[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.qibebt.ac.cn/handle/337004/6091
Collection生物传感技术团队(过去)
Affiliation1.Ocean Univ China, Minist Educ, Key Lab Marine Chem Theory & Technol, Qingdao 266100, Peoples R China
2.Ocean Univ China, Coll Chem & Chem Engn, Qingdao 266100, Peoples R China
3.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Lab Biosensing, Qingdao 266101, Peoples R China
4.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Key Lab Biofuels, Qingdao 266101, Peoples R China
Recommended Citation
GB/T 7714
Song, Jianxia,Liang, Bo,Han, Dongfei,et al. Bacterial cell-surface displaying of thermo-tolerant glutamate dehydrogenase and its application in L-glutamate assay[J]. ENZYME AND MICROBIAL TECHNOLOGY,2015,70(1):72-78.
APA Song, Jianxia.,Liang, Bo.,Han, Dongfei.,Tang, Xiangjiang.,Lang, Qiaolin.,...&Liu, Aihua.(2015).Bacterial cell-surface displaying of thermo-tolerant glutamate dehydrogenase and its application in L-glutamate assay.ENZYME AND MICROBIAL TECHNOLOGY,70(1),72-78.
MLA Song, Jianxia,et al."Bacterial cell-surface displaying of thermo-tolerant glutamate dehydrogenase and its application in L-glutamate assay".ENZYME AND MICROBIAL TECHNOLOGY 70.1(2015):72-78.
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