Photocontrol of immobilized trypsin activity

✍ Scribed by Yoshiaki Nakmoto; Morie Nishida; Isao Karube; Shuichi Suzuki

• Publisher: John Wiley and Sons
• Year: 1977
• Tongue: English
• Weight: 379 KB
• Volume: 19
• Category: Article
• ISSN: 0006-3592
• DOI: 10.1002/bit.260190803

✦ Synopsis

Abstract

Trypsin was coupled on an agarose gel which was modified with a spiropyran compound. The trypsin–spiropyran (agarose) gel showed reverse photochromism. The activity of the trypsin–spiropyran gel in the dark was 12% of that of native trypsin, and it was higher than that under visible light. The apparent Michaelis constant of the trypsin–spiropyran gel in the dark was larger than that under visible light. On the other hand, the maximum velocity in the dark was higher than that under visible light. The optimum pH of the trypsin–spiropyran gel in the dark was the same as that under visible light. Immobilized trypsin was stable in the pH range from 3 to 9. The trypsin–spiropyran gel was more stable against heat than the native trypsin.