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Expression, immobilization and enzymatic properties of glutamate decarboxylase fused to a cellulose-binding domain.
MedLine Citation:
PMID:  22312257     Owner:  NLM     Status:  PubMed-not-MEDLINE    
Abstract/OtherAbstract:
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(3)N(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.
Authors:
Hyemin Park; Jungoh Ahn; Juwhan Lee; Hyeokwon Lee; Chunsuk Kim; Joon-Ki Jung; Hongweon Lee; Eun Gyo Lee
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Publication Detail:
Type:  Journal Article     Date:  2011-12-28
Journal Detail:
Title:  International journal of molecular sciences     Volume:  13     ISSN:  1422-0067     ISO Abbreviation:  Int J Mol Sci     Publication Date:  2012  
Date Detail:
Created Date:  2012-02-07     Completed Date:  2012-10-02     Revised Date:  2013-05-29    
Medline Journal Info:
Nlm Unique ID:  101092791     Medline TA:  Int J Mol Sci     Country:  Switzerland    
Other Details:
Languages:  eng     Pagination:  358-68     Citation Subset:  -    
Affiliation:
Biotechnology Process Engineering Center, KRIBB, Daejeon 305-600, Korea; E-Mails: gohworld@kribb.re.kr (H.P.); ahnjo@kribb.re.kr (J.A.); jhlee@kribb.re.kr (J.L.); tntn7616@kribb.re.kr (H.L.); chskim@kribb.re.kr (C.K.); jkjung@kribb.re.kr (J.-K.J.); hwlee@kribb.re.kr (H.L.).
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