Effects of Two Trypsin Inhibitors on Trypsin in Activity and Structure

Abstract

Two reversible trypsin inhibitors, Kunitz trypsin inhibitor (KTI) and Bowman-Birk trypsin inhibitor (BBI) were compared to find the more optimal one as the inhibit factor during trypsin immobilization. Fluorescence spectroscopy, UV–visible absorption spectroscopy and circular dichroism (CD) spectroscopy were used to explore the effects of the two inhibitors on trypsin in activity and structure. The results showed that both inhibitors combined with trypsin in 1:1. CD circular dichroism spectroscopy showed that KTI and BBI led to different changes in trypsin second structure. The results can help us find out the mechanism between the two inhibitors and trypsin and select the more optimal inhibitor in trypsin immobilization.

Determination of protease inhibitors, glycinin, and beta‐conglycinin in soybeans and their relationships

“…This means for the same unit mass, KTI contributes more to the trypsin inhibition than BBI. Even though both KTI and BBI bind to trypsin at the same molar ratio of 1:1, the two inhibitors cause different structural changes of trypsin, which could lead to different inhibitory activity (Dong et al, 2014). The observed different degrees of trypsin inhibition might be, to some extent, due to their different binding coefficients with trypsin.…”