Stabilization of Enzyme by Using Hydrophobic Ligands.

• Ota Hideyuki

  Department of Chemical Science and Engineering, Graduate School of Engineering Science, Osaka University

• Yamahara Katsuhito

  Department of Chemical Science and Engineering, Graduate School of Engineering Science, Osaka University

• Kuboi Ryoichi

  Department of Chemical Science and Engineering, Graduate School of Engineering Science, Osaka University

Bibliographic Information

Other Title

• Stabilization of Enzyme by Using Hydrop

Abstract

The protection (stabilization) effect of various hydrophobic ligands on the denaturation and aggregation of carbonic anhydrase from bovine (CAB) has been quantitatively investigated under various heat stress conditions. In a limited temperature range (40∼60°C), where the protein was only partially denatured and the local hydrophobicities (LH) of CAB were positive effective stabilization of the protein is achieved by the addition of various ligands. The importance of balance between hydrophobic head and hydrophilic tail of the ligands is hypothesized.

Journal

• JOURNAL OF CHEMICAL ENGINEERING OF JAPAN

  JOURNAL OF CHEMICAL ENGINEERING OF JAPAN 31 (1), 118-122, 1998

  The Society of Chemical Engineers, Japan

Keywords

• Hydrophobic Ligands
• Stabilization
• CAB
• Denaturation
• Aggregation
• Heat Stress Condition
• Hydrophobic Head
• Hydrophilic Tail

Details

• CRID: 1390001204566806656
• NII Article ID: 10002064990
• NII Book ID: AA00709658
• DOI: 10.1252/jcej.31.118
• COI: 1:CAS:528:DyaK1cXhvV2qs7s%3D
• ISSN: 18811299
• ISSN: 00219592
• NDL BIB ID: 4427722
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I4427722
• Web Site: http://www.jstage.jst.go.jp/article/jcej/31/1/31_1_118/_pdf
• Text Lang: en
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed