Journal of Food and Nutrition Research
ISSN (Print): 2333-1119 ISSN (Online): 2333-1240 Website: http://www.sciepub.com/journal/jfnr Editor-in-chief: Prabhat Kumar Mandal
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Journal of Food and Nutrition Research. 2015, 3(3), 152-156
DOI: 10.12691/jfnr-3-3-4
Open AccessArticle

Effect of Rice–based Fat Substitute on Gelation of Myofibrillar Proteins

Yuling Yang1, , Yuan You1, Xiaobei Peng1, Yinji Chen1 and Yun Ma1

1College of Food Science and Engineering, Nanjing University of Finance and Economics/ Key Laboratory of Grain and Oils Quality Control and Deep-Utilizing Technology of Jiangsu Province, Nanjing, 210046, China

Pub. Date: March 02, 2015

Cite this paper:
Yuling Yang, Yuan You, Xiaobei Peng, Yinji Chen and Yun Ma. Effect of Rice–based Fat Substitute on Gelation of Myofibrillar Proteins. Journal of Food and Nutrition Research. 2015; 3(3):152-156. doi: 10.12691/jfnr-3-3-4

Abstract

This study was designed to investigate the effect of rice–based fat substitute (FS) on heat-induced gelation of myofibrillar proteins (MP) from chicken breast muscle. The secondary structure, calorimetric and rheological attributes (α-helix, β-sheet, heat flow and G’) of FS and MP mixtures were measured during gel formation. The results indicated that the addition of FS led to easier denaturation of myosin but delayed denaturation of actin. The α-helix content in the MP-FS mixture was lower than that of MP, whilst β-sheet content in the MP-FS mixture was higher than that of MP when heating temperature was higher than 60 °C, indicating that the addition of FS could promoted MP molecules unfolding and aggregating at higher temperature. The G’ value of the MP-FS mixture was higher than that of MP during heating. The initial gelling temperatures of the MP sample and the MP-FS sample were 42 °C according to G’ curves. The hardness value of the MP-FS gel was higher than that of the MP gel at temperature over 60 °C, and reached the maximum value at . Scanning electron microscopy showed that FS changed the microstructure of MP gel. It was concluded that the addition of FS promoted MP molecule unfolding, aggregating and gelling at heating temperature over 60 °C, but FS did not change the initial gelling temperature of MP molecules and the optimal gel-forming temperature.

Keywords:
myofibrillar proteins fat substitute gelation gel properties

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References:

[1]  Ziegler, GR. - Foededing, EA. The gelation of proteins. Advances in Food and Nutrition Research, 34, 1990, 203-280.
 
[2]  Sano, T. - Noguchi, SF. - Tsuchiya, T. - Matsumoto, JJ. Dynamic viscoelastic behavior of natural actomyosin and myosin during thermal gelation. Journal of Food Science, 53(3), 1988, 924-928.
 
[3]  Stabursvik, E. - Martens, H. Thermal denaturation of proteins in post rigor muscle tissue as studied by differential scanning calorimetry. Science of the Food and Agriculture, 31, 1980, 1034-1042.
 
[4]  Wright, DJ. - Wilding, P. Different scanning calorimetric study of muscle and its proteins, myosin and its subfragments. Journal of the Science of Food and Agriculture 35, 1984, 357-372.
 
[5]  Wang, SF. - Smith, DM. Dynamic rheological properties and secondary structure of chicken breast myosin as influenced by isothermal heating. Journal of Agricultural and Food Chemistry, 42, 1994a, 1434-1439.
 
[6]  Lesiów, T. - Xiong, YL. Mechanism of rheological changes in poultry myofibrillar proteins during gelation. Avian and Poultry Biology Reviews 12(4), 2001, 137-149.
 
[7]  Yongsawatdigul, J. - Park, JW. Thermal denaturation and aggregation of threadfin bream actomyosin. Food Chemistry, 83, 2003, 409-416.
 
[8]  Hemung, BO. - Eunice, CY. - Chan, L. - Yongsawatdigul, J. Thermal stability of fish natural actomyosin affects reactivity to cross-linking by microbial and fish transglutaminases. Food Chemistry, 111(2), 2008, 439-446.
 
[9]  Liu, R. - Zhao, SM. - Liu, YM. - Yang, H. - Xiong, SB. - Xie, BJ. - Qin, LH. Effect of pH on the gel properties and secondary structure of fish myosin. Food Chemistry, 121(1), 2010, 196-202.
 
[10]  Amako, D. - Xiong, YL. Effects of carrageenan on thermal stability of proteins from chicken thigh and breast muscles. Food Research International, 34, 2001, 247-253.
 
[11]  Chin, KB. - Go, MY. - Xiong, YL. Effect of soy protein substitution for sodium caseinate on the transglutaminate-induced cold and thermal gelation of myofibrillar protein. Food Research International, 42(8), 2009, 941-948.
 
[12]  Hong, GP. - Chin, KB. Effects of microbial transglutaminase and sodium alginate on cold-set gelation of porcine myofibrillar protein with various salt levels. Food Hydrocolloid, 24, 2010, 444-451.
 
[13]  Yang, YL. - Xu, SY. Roles of components of rice-based fat substitute in gelation. Food Research International, 40(9), 2007, 1155-1160.
 
[14]  Hsu, SY. - Sun, LY. Comparisons on 10 non-meat protein fat substitutes for low-fat Kung-wans. Journal of Food Engineering, 74, 2006, 47-53.
 
[15]  Ju, J. - Mittal, GS. Physical properties of various starch based fat-substitutes. Journal of Food Processing and Preservation, 19, 1995, 361-383.
 
[16]  Xiong, YL. A comparison of the reological characteristics of different fractions of chichen myofibrillar proteins. Journal of Food Biochemistry, 16, 1992, 217-227.
 
[17]  Hizukuri, S. - Takeda, Y. - Yasuda, M. Multi-branched nature of amylose and the action of debranching enzymes. Carbohydrate Research, 94(2), 1981, 205-213.
 
[18]  Xiong, YL. - Brekke, CJ. Thermal transitions of salt-soluble protein from pre- and postrigor chicken muscles. Journal of Food Science, 55(6), 1990, 1540-1543.
 
[19]  Chen, HH. - Xu, SY. - Wang, Z. Interaction between flaxseed gum and meat protein. Journal of Food Engineering, 80(4), 2007, 1051-1059.
 
[20]  Ma, F. - Chen, CG. - Zheng, L. - Zhou, CL. - Cai, KZ. - Han, Z. Effect of high pressure processing on the gel properties of salt-soluble meat protein containing CaCl2 and κ-carrageenan. Meat Science, 95(1), 2013, 22-26.
 
[21]  Ramirez, JC. - Addo, K. - Xiong, YL. Gelation of mixed myofibrillar/wheat gluten proteins treated with microbial transglutaminase. Food Research International, 38, 2005, 1143-1149.
 
[22]  Wang, CH. - Damodaran, S. Thermal gelation of globular proteins, influence of protein conformation on gel strength. Journal of Agricultural and Food Chemistry, 39(3), 1991, 433-438.
 
[23]  Li, XK. - Xia, WS. Effects of chitosan on the gel properties of salt-soluble meat proteins from silver carp. Carbohydrate Polymers, 82, 2010, 958-964.
 
[24]  Verbeken, D. - Neirinck, N. - Meeren, PVD. - Dewettinck, K. Influence of k-carrageenan on the thermal gelation of salt-soluble meat proteins. Meat Science, 70, 2005, 161-166.
 
[25]  Yang, YL. - Zhou, GH. - Xu, XL. - Wang, Y. Rheological Properties of Myosin–Gelatin Mixtures. Journal of Food Science, 72(5), 2007, 270-275.
 
[26]  Sun, JX. - Wu, Z. - Xu, XL. - Li, P. Effect of peanut protein isolate on functional properties of chicken salt-soluble proteins from breast and thigh muscles during heat-induced gelation. Meat Science, 91, 2012, 88-92.