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. 2016 Feb 29;25(1):21–26. doi: 10.1007/s10068-016-0003-0

Changes in properties of white shrimp (Litopenaeus vannamei) protein during thermal denaturation

Ruichang Gao 2, Xueping Feng 2, Wenwen Li 2, Li Yuan 2, Jing Ge 2, Daoli Lu 2, Bin Chen 2, Gang Yu 1,✉
PMCID: PMC6049370  PMID: 30263231

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.

Keywords: Raman spectroscopy, white shrimp, protein, structures, denaturation

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