FOOD SCIENCE ›› 2013, Vol. 34 ›› Issue (21): 30-35.doi: 10.7506/spkx1002-6630-201321007

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Rheological and Raman Spectroscopic Characteristics of Heat-induced Chicken Myofibrillar Protein Gel Influenced by Sodium Substitution and Muscle Type

WANG Peng,CHEN Lin,SUN Jian,KANG Zhuang-li,XIA Tian-lan,XU Xing-lian*,ZHOU Guang-hong   

  1. Key Laboratory of Meat Processing and Quality Control, Ministry of Education, College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China
  • Received:2013-08-26 Revised:2013-10-17 Online:2013-11-15 Published:2013-10-28
  • Contact: XU Xing-lian E-mail:xuxinglian@njau.edu.cn

Abstract:

Gel properties of muscle proteins are affected by the concentration and type of salt. An attempt to partial replacement
of NaCl in myofibrillar protein gelation model through the use of three treatments (0.4 mol/L NaCl + 0.2 mol/L KCl, 0.4 mol/L
NaCl+ 0.1 mol/L MgCl2 and 0.4 mol/L NaCl + 0.5% TPP) in comparison to controls (0.6 mol/L NaCl as normal control and
0.4 mol/L NaCl as low sodium control) was assayed to evaluate textural, rheological and raman spectroscopic characteristics
of heat-induced myofibrillar protein gel from thigh and breast muscles as well as their combination. The results showed
that the texture and rheological parameters of heat-induced breast myofibrillar protein gel were higher than those of heatinduced
thigh myofibrillar protein gel. The lower gel-forming capacity of thigh myofibrillar protein could be improved by
protein-protein interactions as a result of partial replacement of NaCl with KCl or TPP. Raman spectroscopic studies showed
a higher percentage of β-sheet in breast myofibrillar proteins than thigh myofibrillar proteins and significantly increased
percentage of β-sheet in myofibrillar proteins from mixed breast and thigh muscles with partial replacement of NaCl
compared with single thigh muscle. Overall, the properties of heat-induced myofibrillar protein gels from breast and thigh
muscles can be regulated by protein-protein interactions under partial replacement of NaCl.

Key words: sodium substitution, myofibrillar protein, heat-inducted gelation, rheology, Raman spectroscopy

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