The changes and relationship of structure and functional properties of rabbit myosin during heat-induced gelation

被引：23

作者：

Han, Minyi ^{[1
,2
]}

Wu, Ye ^{[1
]}

Wang, Peng ^{[1
]}

Xu, Xinglian ^{[1
]}

Zhou, Guanghong ^{[1
]}

机构：

[1] Nanjing Agr Univ, Minist Agr, Key Lab Anim Prod Proc, Nanjing 210095, Jiangsu, Peoples R China

[2] Hebei Univ Sci & Technol, Coll Biosci & Bioengn, Shijiazhuang 050018, Peoples R China

来源：

CYTA-JOURNAL OF FOOD | 2015年 / 13卷 / 01期

关键词：

temperature; secondary structure; water holding capacity; hardness; rheological properties; PORCINE MYOFIBRILLAR PROTEIN; CIRCULAR-DICHROISM; RHEOLOGICAL PROPERTIES; SECONDARY STRUCTURE; ELECTRON-MICROSCOPY; RAMAN-SPECTROSCOPY; THERMAL GELATION; GELS; MUSCLE; PH;

D O I：

10.1080/19476337.2014.913687

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

The objective of this study was to track the changes and the relationship between structure and functional properties of rabbit myosin during heat-induced gelation, and to provide more insight into the gelation properties of rabbit myosin. Storage modulus (G') and loss modulus (G '') during the heat-induced gelation process were measured by a rheometer, and the water holding capacity (WHC) and hardness of the heat-induced gel were measured by centrifugation method and texture analyzer, respectively. The quantitative analysis of secondary structural content was performed by circular dichroism (CD). The CD data were fitted to three secondary structures, which were alpha-helix, beta-sheet, and random coil. The results showed that the WHC, hardness, G', G '', beta-sheet, and random coil increased with the increase of temperature, while the alpha-helix decreased. The changes of structural properties of myosin determined the functional properties during the heat-induced gelation process, and they had a very strong correlation.

引用

页码：63 / 68

页数：6

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