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

被引：23

作者：

Gao, Ruichang ^{[2
]}

Feng, Xueping ^{[2
]}

Li, Wenwen ^{[2
]}

Yuan, Li ^{[2
]}

Ge, Jing ^{[2
]}

Lu, Daoli ^{[2
]}

Chen, Bin ^{[2
]}

Yu, Gang ^{[1
]}

机构：

[1] Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, Guangzhou 510300, Guangdong, Peoples R China

[2] Jiangsu Univ, Sch Food & Biol Engn, Zhenjiang 212013, Peoples R China

来源：

FOOD SCIENCE AND BIOTECHNOLOGY | 2016年 / 25卷 / 01期

关键词：

Raman spectroscopy; white shrimp; protein; structures; denaturation; WATER-HOLDING CAPACITY; MERLUCCIUS L. MUSCLE; STRUCTURAL-CHANGES; RAMAN-SPECTROSCOPY; QUALITY; MEAT; GELS;

D O I：

10.1007/s10068-016-0003-0

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

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 50A degrees C. A decrease in the percentage of alpha-helices accompanied by an increase in the percentage of beta-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.

引用

页码：21 / 26

页数：6

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