Abstract
Changes in white shrimp (Litopenaeus vannamei) protein during thermal denaturation were studied using Raman spectroscopy and isotopic H/D exchange. Denaturation of shrimp protein began after heating for 10 min at 50°C. A decrease in the percentage of α-helices accompanied by an increase in the percentage of β-sheets occurred while the total percentage of disordered structures increased. With extension of the exchange time, the relative intensity of the O-D bond increased, accompanied by a higher relative O-D bond intensity for heated shrimp, compared with unheated shrimp. H/D exchange revealed a higher rate of deuteration kinetics in heated shrimp than for unheated shrimp, especially during the first 2 h, consistent with water loss from denatured white shrimp protein. Physical property changes in muscle tissue can be caused by changes in hydrogen bonding and hydrophobicity during thermal processes.