Kinetic Analysis of the Inhibition by Melanoidin of Trypsin.

• HIRANO Miyuki

• MIURA Masayo

• GOMYO Toshiharu

抄録

The inhibition by melanoidin of trypsin was investigated in a kinetic approach. Melanoidin was prepared by the Maillard reaction between D-glucose and glycine, and BANA was used as a substrate. The inhibition was found to follow a non-competitive mode with a K_i of 5.8% and to be exerted through an electrostatic interaction between melanoidin and trypsin. Approximately 20% of the activity of trypsin survived even at a greatly increased concentration of melanoidin. The inhibiting mechanism of melanoidin might be due to an allosteric effect, which was probably different from a proteinaceous inhibitor such as ovoinhibitor diminishing trypsin-activity completely. The melanoidin molecule was thought to trap a great number of trypsin molecules, binding them and reducing their activity.

収録刊行物

• Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ

  Ｂｉｏｓｃｉｅｎｃｅ，　Ｂｉｏｔｅｃｈｎｏｌｏｇｙ，　ａｎｄ　Ｂｉｏｃｈｅｍｉｓｔｒｙ 60 (3), 458-462, 1996

  公益社団法人 日本農芸化学会

キーワード

• trypsin
• chymotrypsin
• melanoidin
• inhibition
• Maillard reaction

詳細情報

• CRID: 1390001206475854080
• NII論文ID: 110002678032
• NII書誌ID: AA10824164
• DOI: 10.1271/bbb.60.458
• COI: 1:CAS:528:DyaK28XhvFygtrY%3D
• ISSN: 13476947
• ISSN: 09168451
• ISSN: http://id.crossref.org/issn/09168451
• Web Site: http://www.tandfonline.com/doi/pdf/10.1271/bbb.60.458
• 本文言語コード: en
• データソース種別:
  • JaLC
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可