Binding behavior and antioxidant study of spice extract piperine with respect to meat myoglobin

Abstract

static quenching. After binding to PIP, the α-helix content of Mb decreased by about 5%. Synchronous fluorescence results indicate that PIP is closer to Trp, and MD simulations also demonstrate that PIP enters the hydrophobic cavity of Mb and binds stably. This explains the structural changes in proteins that lead to changes in antioxidant properties. The results of this study provide a reference for the quality control of additives of plant origin in the processing and storage of meat and meat products.

Topics & Concepts