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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

Authors 

Hye-Min ParkJungoh AhnJoo Hwan LeeHyeok Won LeeChunsuk KimJoon Ki JungHong-Weon LeeEun Gyo Lee

Publisher 

MDPI AG

Issue Date 

2012

Citation 

International Journal of Molecular Sciences, vol. 13, no. 1, pp. 358-368

Keywords 

Cellulose-binding domainFusion proteinGADImmobilization

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.

ISSN 

1422-0067

Link 

http://dx.doi.org/10.3390/ijms13010358

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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