Effect of pH on NMR Relaxometry and Chicken Myosin Gel Properties


  • Qiuhui Zhang College of Food, Shenyang Agricultural University, Shenyang, Liaoning Province 110866
  • Xiqing Yue
  • Miaoyun Li
  • Gaiming Zhao College of Food Science and Technology, Henan Agricultural University, Zhengzhou, Henan Province, 450002
  • Xianqing Huang


chicken myosin, gel property, pH, NMR


The effect of pH on low-field nuclear magnetic resonance (NMR) relaxometry datas, water holding capacity (WHC), gel strength, and microstructure of chicken myosin gel was investigated. There was a positive and significant correlation between WHC and gel strength. The WHC of the myosin gel significantly increased as the pH deviated from the myosin isoelectric point. T22 increased to 35.10ms at pH 6.5, indicating that the free water transformed to mobile water, which led to better WHC of chicken myosin gels. Maximum gel strength (30.78g) was obtained at pH 6.5. Scanning electron micrographs (SEM) showed that the mobility of water in the protein gel network correlated to the gel microstructure. A compact and uniform chicken myosin gel was acquired at pH 6.5.



Bertram H.C., Kristensen M.. “Functionality of myofibrillar proteins as affected by pH, ionic strength and heat treatment --a low-field NMR studyâ€, Meat Science, vol. 68, no. 2, pp. 249-256, 2004.

Bertram H.C., Karlsson A.H., Rasmusen M., Pedersen O.D., Donstrup S., Andersen H.J.. “Origin of multiexponential T2 relaxation in muscle myowaterâ€, Journal of Agricultural and Food chemistry, vol. 49, no. 6, pp. 3092-3100, 2004.

Brown R.J.S., Capozzi F., Cavani C., Cremonini M.A., Petracci M., Placucci G.. “Relationships between 1H NMR relaxation data and some technological parameters of meat: A chemometric approachâ€, Journal of Magnetic Resonance, vol. 147, no. 1, pp. 89-94, 2000.

Cao Y.Y., Xia T.L., Zhou G.H., Xu X.L.. “The mechanism of high pressure-induced gels of rabbit myosin. Innovative Food Science & Emerging Technologiesâ€, vol. 16, pp. 41-46, 2012.

Damodaran S.. Amino acids, peptides, and proteins. Marcel Dekker, USA, 1996.

Gornall A.G.. “Determination of serum proteins by means of biured reactionâ€, J Biol Chem, vol. 177, pp. 751, 1949.

Han M.Y., Zhang Y.J., Fei Y., Xu X.L., Zhou G.H.. “Effect of microbial transglutaminase on NMR relaxometry and microstructure of pork myofibrillar protein gelâ€, Eur Food Res Technol, vol. 228, pp. 665-670, 2009.

Hermansson1 A.M., Harbitz O., Langton M.. “Formation of two types of gels from bovine myosinâ€. Journal of the Science of Food and Agriculture, vol. 37, no. 1, pp. 69-84, 1986.

Herrero A.M.. “Raman spectroscopy a promising technique for quality assessment of meat and fish: A reviewâ€. Food Chemistry, vol. 107, no. 4, pp. 1642-1651, 2008.

Hills B.P., Takacs S.F., Belton P.S.. “The effects of proteins on the proton N. M. R. transverse relaxation times of waterâ€, Molecular Physics, vol. 67, no. 4, pp. 903-937, 1989.

Hinrichs R., Götz J., Noll M., Wolfschoon A., Eibel H., Weisser H.. “Characterisation of the water-holding capacity of fresh cheese samples by means of low resolution nuclear magnetic resonanceâ€, Food Research International, vol. 37, no. 7, pp. 667-676, 2004.

Kocher P.N., Foegeding E.A.. “Microcentrifuge-based method for measuring water-holding of protein gelsâ€, Journal of Food Science, vol. 58, pp. 1040-1046, 1993.

Kristinsson H.G., Hultin H.O.. “Role of pH and ionic strength on water relationships in washed minced chicken-breast muscle gelsâ€, Journal of Food Science, vol. 68, no. 3, pp. 917-922, 2003.

Laemmli U.K.. “Cleavage of structural proteins during the assembly of the head of bacerio phage T4â€, Nature, vol. 227, pp. 680-685, 1970.

Lanier T.C., Carvajal P., Yongsawatdigul J.. Surimi gelation chemistry, Marcel Dekker, USA, 2004.

Lin T.M., Park J.W.. “Solubility of salmon myosin as affected by conformational changes at various ionic strengths and Phâ€, Journal of Food Science, vol. 63, no. 2, pp. 215-218, 1998.

Liu R., Zhao S.M., Liu Y.M., Yang H., Xiong S.B., Xie B.J., Qin L.H.. “Effect of pH on the gel properties and secondary structure of fish myosinâ€, Food Chemistry, vol. 121, pp. 196-202, 2010.

Liu R., Zhao S.M., Xiong S.B., Xie B.J., Qin L.H.. “Role of secondary structures in the gelation of porcine myosinb at different pH valuesâ€, Meat Science, vol. 80, pp. 632-639, 2008.

Liu R., Zhao S.M., Xiong S.B., Xie B.J.. “Studies on fish and pork paste gelation by dynamic rheology and circular dichroismâ€, Journal of Food Science, vol. 27, no. 7, pp. 399-403, 2007.

Nauss K.M., Kitagawa S., Gergely J.. “Pyrophosphate Binding to and Adenosine Triphosphatase Activity of Myosin and Its Proteolytic Fragmentsâ€, Journal of Biological Chemistry, vol. 244, no. 3, pp. 755-765, 1969.

Saguera E., Forta N., Alvarezb P.A., Sedmanb J., Ismailb A.A.. “Structure–functionality relationships of porcine plasma proteins probed by FTIR spectroscopy and texture analysisâ€, Food Hydrocolloids, vol. 22, no. 3, pp. 459-467, 2008.

Starr R., Offer G.. “Polypeptide chains of intermediate molecular weight in myosin preparationsâ€,FEBS Letters, vol. 15, no. 1, pp. 40-44, 1971.

Surel O., Famelart M.H.. “Heat induced gelation of acid milk:balance between weak and covalent bondsâ€, Journal of Dairy Research, vol. 70, pp. 253-256, 2003.

Trout G.R.. “Techniques for measuring water-binding capacity in muscle foods—A review of methodologyâ€, Meat Science, vol. 23, no. 4, pp. 235-252, 1988.

Wang S.F., Smith D.M.. “Heat induced denaturation and rheological properties of chicken breast myosin and F-actin in the presence and absence of pyrophosphateâ€, Journal of Agricultural Food Chemistry. vol. 42, pp. 2665-2670, 1994a.

Wang S.F., Smith D.M.. “Dynamic rheological properties and secondary structure of chicken breast myosin as influenced by isothermal heatingâ€, Journal of Agricultural Food Chemistry, vol. 42, pp. 1434-1439, 1994c.

Westphalen A.D., Briggs J.L., Lonergan S.M.. “Influence of pH on rheological properties of porcine myofibrillar protein during heat induced gelationâ€, Meat Science, vol. 70, pp. 293-299, 2005.

Yongsawatdigul J., Sinsuwan S.. “Aggregation and conformational changes of tilapia actomyosin as affected by calcium ion during settingâ€, Food Hydrocolloids, vol. 21, pp. 359-367, 2007.

Zhang L.L., Xue Y., Xu J., Li Z.J., Xue C.H.. “Effects of high-temperature treatment (≥100℃) on Alaska Pollock (Theragra chalcogramma) surimi gelsâ€, Journal of Food Engineering, vol. 115, pp. 115-120, 2013.




How to Cite

Zhang, Q., Yue, X., Li, M., Zhao, G., & Huang, X. (2014). Effect of pH on NMR Relaxometry and Chicken Myosin Gel Properties. Asian Journal of Agriculture and Food Sciences, 2(4). Retrieved from https://www.ajouronline.com/index.php/AJAFS/article/view/1487




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