Microwave radiation accelerates trypsin-catalyzed peptide hydrolysis at constant bulk temperature

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• 作者：Sina Atrin Mazinani ; Benjamin DeLong ; Hongbin Yan ; ^{tyan@brocku.ca" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Microwave heating ; Conventional heating ; Trypsin ; Casein ; Enzyme activity
• 刊名：Tetrahedron Letters
• 出版年：2015
• 出版时间：14 October 2015
• 年：2015
• 卷：56
• 期：42
• 页码：5804-5807
• 全文大小：899 K

文摘

The influence of microwave radiation on trypsin activity was explored using a CEM CoolMate apparatus at a constant bulk temperature. Digestion of N伪(±)-benzoyl-d/l-arginine-4-nitroanilide hydrochloride, azocasein and casein catalyzed by trypsin from the bovine pancreas was found to be accelerated when the reaction mixture was exposed to microwave radiation, while the bulk temperature was maintained constant through external cooling. Trypsin activity was found to be increased significantly when the reaction mixture was irradiated with microwave at a constant temperature. Cyclic dichroism measurement of trypsin exposed to microwave radiation suggests that there are changes in the secondary structure of trypsin exposed to microwave and conventional heating, however, these changes are presumably due to self-cleavages of trypsin.