Earticle

초록

영어

The SGNH superfamily is characterized by four highly conserved sequence blocks containing serine (S), glycine (G), asparagine (N), and histidine (H) residues. High specificities of SGNH hydrolases could make them appropriate for a wide variety of applications such as preparations of chiral compounds and enantiomeric resolutions. Here, acyl-CoA thioesterase1 precursor from L. innocus CLIP 11262 was used as a model enzyme to investigate its industrial applications of SGNH hydrolase family. Especially, cross-linked enzyme aggregates (CLEAs) from this enzyme were investigated for the immobilization process. Efficient cross-linking was observed when using 80%-saturation ammonium sulfate precipitations followed by crosslinking with 0.5%(v/v) glutaraldehyde for 12h-14h. The CLEA product was much more resistant to denaturation than the free soluble enzyme. For example, while soluble enzyme retained only 20% of its initial activity after 1 h incubation at 80 °C, 75% of activity in CLEA product was observed after 2h of incubation. In addition, after 15 day of storage at 4℃, the LI22-CLEA retained more than 85% of its initial activity. We are currently investigating biochemical and biophysical properties of LI22-CLEA using several biochemical and biophysical approaches including scanning electron microscopy (SEM).

키워드

저자

• Seul Gi KIM [ Dept. of Molecular Science and Technology, Ajou University, Suwon, 443-749. ]
• Song Yi BAE [ Dept. of Molecular Science and Technology, Ajou University, Suwon, 443-749. ]
• Nam Yong KIM [ Dept. of Molecular Science and Technology, Ajou University, Suwon, 443-749. ]
• So Hyun PARK [ Dept. of Molecular Science and Technology, Ajou University, Suwon, 443-749. ]
• T. Doohun KIM [ Dept. of Molecular Science and Technology, Ajou University, Suwon, 443-749. ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576