Earticle

초록

영어

Glutamic acid decarboxylase (GAD) catalyzes the decarboxylation of L-glutamate to gamma-amino butyric acid (GABA), which is not only a chief inhibitory neurotransmitter in human nervous system but also a monomer for polyamide 4, a new attractive biodegradable material.
Therefore, GAD is of interest in large-scale production of GABA and polyamide 4. In this approach, a 6xHis tag was fused to GAD at the N-terminus and overexpressed in E. coli. However, overexpression of GAD resulted in the formation of inclusion body. Efforts were endeavored to increase the amount of soluble enzyme, 0.1 g/l pyridoxine in the culture proved to be the most efficient for the purpose. On the other hand, the activity of GAD was only detected at acidic pH, which limits the reaction at relatively low concentration of the substrate. Since the
C-terminal amino acid residues are considered to be responsible for the inactivation of this enzyme at neutral pH, C-terminal residues were truncated for wider pH range of GAD.

키워드

저자

• Ngoc Anh Thu HO [ Dept. of Chemical & Biochemical Engineering, Dongguk University, Seoul, 100-715. ]
• Chen Yuan HOU [ Dept. of Chemical & Biochemical Engineering, Dongguk University, Seoul, 100-715. ]
• Kee Hoon WON [ Dept. of Chemical & Biochemical Engineering, Dongguk University, Seoul, 100-715. ]
• Taek Jin KANG [ Dept. of Chemical & Biochemical Engineering, Dongguk University, Seoul, 100-715. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576