Expression, immobilization and enzymatic properties of glutamate decarboxylase fused to a cellulose-binding domain = CBD 결합도메인 융합 글루탐산탈탄산효소의 발현 및 고정화효소 반응

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Title
Expression, immobilization and enzymatic properties of glutamate decarboxylase fused to a cellulose-binding domain = CBD 결합도메인 융합 글루탐산탈탄산효소의 발현 및 고정화효소 반응
Author(s)
Hye-Min Park; Jungoh AhnJoo Hwan LeeHyeok Won Lee; Chunsuk Kim; Joon Ki Jung; Hong-Weon LeeEun Gyo Lee
Bibliographic Citation
International Journal of Molecular Sciences, vol. 13, no. 1, pp. 358-368
Publication Year
2012
Abstract
Escherichia coli-derived glutamate decarboxylase (GAD), an enzyme that catalyzes the conversion of glutamic acid to gamma-aminobutyric acid (GABA), was fused to the cellulose-binding domain (CBD) and a linker of Trichoderma harzianum endoglucanase II. To prevent proteolysis of the fusion protein, the native linker was replaced with a S 3N 10 peptide known to be completely resistant to E. coli endopeptidase. The CBD-GAD expressed in E. coli was successfully immobilized on Avicel, a crystalline cellulose, with binding capacity of 33 ± 2 nmol CBD-GAD/g Avicel and the immobilized enzymes retained 60% of their initial activities after 10 uses. The results of this report provide a feasible alternative to produce GABA using immobilized GAD through fusion to CBD.
Keyword
Fusion proteinGADImmobilizationCellulose-binding domain
ISSN
1422-0067
Publisher
MDPI
DOI
http://dx.doi.org/10.3390/ijms13010358
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > BioProcess Engineering Center > 1. Journal Articles
Division of Bio Technology Innovation > 1. Journal Articles
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