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Int. J. Mol. Sci. 2012, 13(1), 358-368; doi:10.3390/ijms13010358

Expression, Immobilization and Enzymatic Properties of Glutamate Decarboxylase Fused to a Cellulose-Binding Domain

Biotechnology Process Engineering Center, KRIBB, Daejeon 305-600, Korea
These authors contributed equally to this work.
Author to whom correspondence should be addressed.
Received: 14 November 2011 / Revised: 15 December 2011 / Accepted: 19 December 2011 / Published: 28 December 2011
(This article belongs to the Section Biochemistry, Molecular Biology and Biophysics)
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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 S3N10 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 nmolCBD-GAD/gAvicel 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.
Keywords: GAD; cellulose-binding domain; fusion protein; immobilization GAD; cellulose-binding domain; fusion protein; immobilization
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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MDPI and ACS Style

Park, H.; Ahn, J.; Lee, J.; Lee, H.; Kim, C.; Jung, J.-K.; Lee, H.; Lee, E.G. Expression, Immobilization and Enzymatic Properties of Glutamate Decarboxylase Fused to a Cellulose-Binding Domain. Int. J. Mol. Sci. 2012, 13, 358-368.

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