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Alpha-Amylase Immobilization on Epoxy Containing Thiol-Ene Photocurable Materials
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  • Alpha-Amylase Immobilization on Epoxy Containing Thiol-Ene Photocurable Materials
  • Alpha-Amylase Immobilization on Epoxy Containing Thiol-Ene Photocurable Materials
저자명
Cakmakci. Emrah,Danis. Ozkan,Demir. Serap,Mulazim. Yusuf,Kahraman. Memet Vezir
간행물명
Journal of microbiology and biotechnology
권/호정보
2013년|23권 2호|pp.205-210 (6 pages)
발행정보
한국미생물생명공학회
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정기간행물|ENG|
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이 논문은 한국과학기술정보연구원과 논문 연계를 통해 무료로 제공되는 원문입니다.
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기타언어초록

Thiol-ene polymerization is a versatile tool for several applications. Here we report the preparation of epoxide groups containing thiol-ene photocurable polymeric support and the covalent immobilization of ${alpha}$-amylase onto these polymeric materials. The morphology of the polymeric support was characterized by scanning electron microscopy (SEM), and energy dispersive spectroscopy (EDS) coupled with SEM was used to explore the chemical composition. The polymeric support and the immobilization of the enzyme were characterized by FTIR analysis. SEM-EDS and FTIR results showed that the enzyme was successfully covalently attached to the polymeric support. The immobilization efficiency and enzyme activity of ${alpha}$-amylase were examined at various pH (5.0-8.0) and temperature ($30-80^{circ}C$) values. The storage stability and reusability of immobilized ${alpha}$-amylase were investigated. The immobilization yield was $276{pm}1.6$ mg per gram of polymeric support. Enzyme assays demonstrated that the immobilized enzyme exhibited better thermostability than the free one. The storage stability and reusability were improved by the immobilization on this enzyme support. Free enzyme lost its activity completely within 15 days. On the other hand, the immobilized enzyme retained 86.7% of its activity after 30 days. These results confirm that ${alpha}$-amylase was successfully immobilized and gained a more stable character compared with the free one.