Raman spectroscopic study of heat-induced gelation of pork myofibrillar proteins and its relationship with textural characteristic

被引:207
作者
Xu, Xiang-Lian [1 ]
Han, Min-Yi [2 ]
Fei, Ying [1 ]
Zhou, Guang-Hong [1 ]
机构
[1] Nanjing Agr Univ, Coll Food Sci & Technol, Key Lab Meat Proc & Qual Control, Nanjing 210095, Peoples R China
[2] Hebei Univ Sci & Technol, Coll Biosci & Bioengn, Shijiazhuang 050018, Peoples R China
关键词
Raman spectroscopy; Textural properties; Heat-induced gelation; Principal component analysis (PCA); PACIFIC WHITING SURIMI; STRUCTURAL-CHANGES; MICROBIAL TRANSGLUTAMINASE; NMR RELAXOMETRY; SYSTEMS; CONFORMATION; MYOSIN; GEL; PH;
D O I
10.1016/j.meatsci.2010.10.001
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Structural changes, textural properties and their relationships in pork myofibrillar proteins (PMP) were studied by Raman spectroscopy, texture profile analysis (TPA) and principal component analysis (PCA). Raman spectroscopy analysis revealed the occurrence of secondary structural changes in myofibrillar proteins. Modifications in the amide I(1600-1700 cm(-1)) and amide III(1200-1300 cm(-1)) regions indicated a significant (p<0.05) decrease in alpha-helix content, accompanied by a significant (p<0.05) increase in beta-sheets, beta-turns and random coil content. Texture property changes were also determined by TPA. All these features contributed to the formation of strong, irreversible heat-induced gels. The application of a dimensionality reducing technique such as PCA proved to be useful to determine the most influential properties of heat-induced gel. Significant (p<0.05) correlations were found between these structural changes and the textural characteristic (hardness) in the pork myofibrillar proteins system by PCA. (C) 2010 The American Meat Science Association. Published by Elsevier Ltd. All rights reserved.
引用
收藏
页码:159 / 164
页数:6
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