Effect of temperature increase and NaCl addition on aggregation and gel properties of pork myofibrillar protein
Corresponding Author
Zhuang-Li Kang
School of Food Science, Henan Institute of Science and Technology, Xinxiang, PR China
Correspondence
Zhuang-Li Kang, School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, PR China.
Email: [email protected]
Contribution: Conceptualization, Data curation, Methodology, Project administration, Supervision, Validation, Visualization, Writing - review & editing
Search for more papers by this authorLing-hui Kong
School of Food Science, Henan Institute of Science and Technology, Xinxiang, PR China
Contribution: Conceptualization, Supervision, Writing - review & editing
Search for more papers by this authorZai-shang Gao
School of Food Science, Henan Institute of Science and Technology, Xinxiang, PR China
Contribution: Conceptualization, Supervision, Writing - review & editing
Search for more papers by this authorYan-ping Li
School of Food Science, Henan Institute of Science and Technology, Xinxiang, PR China
Food Technologies Faculty of Sumy, National Agrarian University, Sumy, Ukraine
Contribution: Funding acquisition, Project administration, Writing - review & editing
Search for more papers by this authorXiang Li
School of Food Science, Henan Institute of Science and Technology, Xinxiang, PR China
Contribution: Data curation, Methodology, Supervision, Writing - review & editing
Search for more papers by this authorHan-jun Ma
School of Food Science, Henan Institute of Science and Technology, Xinxiang, PR China
Contribution: Conceptualization, Formal analysis, Investigation, Methodology, Validation, Writing - original draft
Search for more papers by this authorCorresponding Author
Zhuang-Li Kang
School of Food Science, Henan Institute of Science and Technology, Xinxiang, PR China
Correspondence
Zhuang-Li Kang, School of Food Science, Henan Institute of Science and Technology, Xinxiang 453003, PR China.
Email: [email protected]
Contribution: Conceptualization, Data curation, Methodology, Project administration, Supervision, Validation, Visualization, Writing - review & editing
Search for more papers by this authorLing-hui Kong
School of Food Science, Henan Institute of Science and Technology, Xinxiang, PR China
Contribution: Conceptualization, Supervision, Writing - review & editing
Search for more papers by this authorZai-shang Gao
School of Food Science, Henan Institute of Science and Technology, Xinxiang, PR China
Contribution: Conceptualization, Supervision, Writing - review & editing
Search for more papers by this authorYan-ping Li
School of Food Science, Henan Institute of Science and Technology, Xinxiang, PR China
Food Technologies Faculty of Sumy, National Agrarian University, Sumy, Ukraine
Contribution: Funding acquisition, Project administration, Writing - review & editing
Search for more papers by this authorXiang Li
School of Food Science, Henan Institute of Science and Technology, Xinxiang, PR China
Contribution: Data curation, Methodology, Supervision, Writing - review & editing
Search for more papers by this authorHan-jun Ma
School of Food Science, Henan Institute of Science and Technology, Xinxiang, PR China
Contribution: Conceptualization, Formal analysis, Investigation, Methodology, Validation, Writing - original draft
Search for more papers by this authorAbstract
Effects of increasing in temperature (56 and 72℃) and NaCl (1%–3%) content on the particle size, zeta potential, gel properties and water distribution of pork myofibrillar protein were studied. At the same NaCl content, the particle size, zeta potential, whiteness and hardness of myofibrillar protein gel at 72℃ were increased significantly compared to 56℃, whereas the cooking yield was decreased significantly (p < .05). At the same temperature, the particle size of myofibrillar protein was decreased significantly with increasing NaCl, whereas the whiteness, cooking yield, and hardness of gel were increased significantly (p < .05). In addition, the mobility of water in the cooked myofibrillar protein gel was decreased with increasing NaCl content and temperature. Overall, increasing the temperature and the NaCl content led to improve gel properties and water holding capacity of myofibrillar protein.
Novelty impact statement
Increased the salt and temperature, particle size, zeta potential of pork myofibrillar protein were increased significantly, the fluidity of water was decreased, and then a better gel network was formed.
CONFLICT OF INTEREST
The authors have declared no conflicts of interest for this article.
REFERENCES
- Ahmad, K. N., Booker, H., & Yu, P. (2015). Effect of heating method on alteration of protein molecular structure in flax seed: Relationship with changes in protein subfraction profile and digestion in dairy cows. Journal of Agricultural and Food Chemistry, 63(4), 1057–1066. https://doi.org/10.1021/jf503575y
- Angsupanich, K., Edde, M., & Ledward, D. A. (1999). Effects of high pressure on the myofibrillar proteins of cod and turkey Muscle. Journal of Agricultural and Food Chemistry, 47(1), 92–99. https://doi.org/10.1021/jf980587p
- AOAC (2000). AOAC, official methods of analysis of AOAC international ( 17th ed.). AOAC International.
- Bertram, H. C., Karlsson, A., Rasmussen, M., Pedersen, O. D., Donstrup, S., & Andersen, H. J. (2001). Origin of multiexponential T2 relaxation in muscle myowater. Journal of Agricultural and Food Chemistry, 49, 3092–3100.
- Bistola, V., Arfaras-Melainis, A., Trogkanis, E., Bakosis, G., Polyzogopoulou, E., Karavidas, I., Ikonomidis, I., Parissis, J., & Karavidas, A. (2020). Safety and efficacy of salt substitution with a low sodium-potassium enriched dietary salt in patients with heart failure with reduced ejection fraction: A pilot study. Clinical Nutrition ESPEN, 35, 90–94. https://doi.org/10.1016/j.clnesp.2019.11.004
- Borisova, M. A., & Oreshkin, E. F. (1992). On the water condition in pork meat. Meat Science, 31, 257–265. https://doi.org/10.1016/0309-1740(92)90056-A
- Chen, X., Tume, R. K., Xu, X., & Zhou, G. (2017). Solubilization of myofibrillar proteins in water or low ionic strength media: Classical techniques, basic principles and novel functionalities. Critical Reviews in Food Science and Nutrition, 57(15), 3260–3280. https://doi.org/10.1080/10408398.2015.1110111
- Chin, K. B., Go, M. Y., & Xiong, Y. L. (2009). Effect of soy protein substitution for sodium caseinate on the transglutaminate-induced cold and thermal gelation of myofibrillar protein. Food Research International, 42(8), 941–948. https://doi.org/10.1016/j.foodres.2009.05.008
- Dai, H., Sun, Y. I., Xia, W., Ma, L., Li, L., Wang, Q., & Zhang, Y. (2021). Effect of phospholipids on the physicochemical properties of myofibrillar proteins solution mediated by NaCl concentration. LWT - Food Science and Technology, 141, 110895. https://doi.org/10.1016/j.lwt.2021.110895
- Gornall, A. G., Bardawill, C. J., & David, M. M. (1949). Determination of serum proteins by means of the biuret reaction. Journal of Biological Chemistry, 177(2), 751–766. https://doi.org/10.1016/S0021-9258(18)57021-6
- Han, M., Wang, P., Xu, X., & Zhou, G. (2014). Low-field NMR study of heat-induced gelation of pork myofibrillar proteins and its relationship with microstructural characteristics. Food Research International, 62(62), 1175–1182. https://doi.org/10.1016/j.foodres.2014.05.062
- Hwang, J., Lai, K., & Hsu, K. (2007). Changes in textural and rheological properties of gels from tilapia muscle proteins induced by high pressure and setting. Food Chemistry, 104(2), 746–753. https://doi.org/10.1016/j.foodchem.2006.11.075
- Kang, Z., Li, B., Ma, H., & Chen, F. (2016). Effect of different processing methods and salt content on the physicochemical and rheological properties of meat batters. International Journal of Food Properties, 19(7), 1604–1615. https://doi.org/10.1080/10942912.2015.1105819
- Kang, Z. L., Zhang, X. H., Li, X., Song, Z. J., Ma, H. J., Lu, F., Zhu, M. M., Zhao, S. M., & Wang, Z. R. (2021). The effects of sodium chloride on proteins aggregation, conformation and gel properties of pork myofibrillar protein Running Head: Relationship aggregation, conformation and gel properties. Journal of Food Science and Technology, 58(6), 2258–2264. https://doi.org/10.1007/s13197-020-04736-4
- Kang, Z. L., Zhu, D., Li, B., Ma, H. J., & Song, Z. J. (2017). Effect of pre-emulsified sesame oil on physical-chemical and rheological properties of pork batters. Food Science and Technology International, 37(4), 620–626. https://doi.org/10.1590/1678-457x.28116
- Khan, M. I., Jo, C., & Tariq, M. R. (2015). Meat flavor precursors and factors influencing flavor precursors–A systematic review. Meat Science, 110, 278–284. https://doi.org/10.1016/j.meatsci.2015.08.002
- Li, C., Liu, D., Zhou, G., Xu, X., Qi, J., Shi, P., & Xia, T. (2012). Meat quality and cooking attributes of thawed pork with different low field NMR T21. Meat Science, 92(2), 79–83. https://doi.org/10.1016/j.meatsci.2011.11.015
- Li, J. G., Chen, Y. H., Dong, X. P., Li, K., Wang, Y. T., Wang, Y., Du, M. T., Zhang, J. J., & Bai, Y. H. (2021). Effect of chickpea (Cicer arietinum L.) protein isolate on the heat-induced gelation properties of pork myofibrillar protein. Journal of the Science of Food and Agriculture, 101(5), 2108–2116.
- Li, Z., Li, M., Du, M., Shen, Q. W., & Zhang, D. (2018). Dephosphorylation enhances postmortem degradation of myofibrillar proteins. Food Chemistry, 245, 233–239. https://doi.org/10.1016/j.foodchem.2017.09.108
- Miyaoka, R., Ando, M., Harada, R., Osaka, H., Samuel, A. Z., Hosokawa, M., & Takeyama, H. (2020). Rapid inspection method for investigating the heat processing conditions employed for chicken meat using Raman spectroscopy. Journal of Bioscience and Bioengineering, 129(6), 700–705. https://doi.org/10.1016/j.jbiosc.2020.01.002
- Park, J. W. (1994). Functional protein additives in surimi gels. Journal of Food Science, 59(3), 525–527. https://doi.org/10.1111/j.1365-2621.1994.tb05554.x
- Paula, M. M. O., Haddad, G. B. S., Rodrigues, L. M., Benevenuto Júnior, A. A., Ramos, A. L. S., & Ramos, E. M. (2019). Effects of PSE meat and salt concentration on the technological and sensory characteristics of restructured cooked hams. Meat Science, 173, 96–103. https://doi.org/10.1016/j.meatsci.2019.02.020
- Petruccelli, S., & Anon, M. C. (1995). Thermal aggregation of soy protein isolates. Journal of Agricultural and Food Chemistry, 43(12), 3035–3041. https://doi.org/10.1021/jf00060a009
- Pretorius, B., & Schonfeldt, H. C. (2018). The contribution of processed pork meat products to total salt intake in the diet. Food Chemistry, 238, 139–145. https://doi.org/10.1016/j.foodchem.2016.11.078
- Promeyrat, A., Daudin, J., Astruc, T., Danon, J., & Gatellier, P. (2013). Kinetics of protein physicochemical changes induced by heating in meat using mimetic models: (2) Effects of fibre type, peroxides and antioxidants. Food Chemistry, 138(4), 2283–2290. https://doi.org/10.1016/j.foodchem.2012.11.134
- Promeyrat, A., Daudin, J., & Gatellier, P. (2013). Kinetics of protein physicochemical changes induced by heating in meat using mimetic models: (1) Relative effects of heat and oxidants. Food Chemistry, 138(1), 581–589. https://doi.org/10.1016/j.foodchem.2012.10.084
- Promeyrat, A., Louet, L. L., Kondjoyan, A., Astruc, T., Santé-Lhoutellier, V., Gatellier, P., & Daudin, J. D. (2011). Combined effect of meat composition and heating parameters on the physicochemical state of proteins. Procedia Food Science, 1, 1118–1125. https://doi.org/10.1016/j.profoo.2011.09.167
- Schmitt, C., Bovay, C., Rouvet, M., Shojaeirami, S., & Kolodziejczyk, E. (2007). Whey protein soluble aggregates from heating with NaCl: Physicochemical, interfacial, and foaming properties. Langmuir, 23(8), 4155–4166.
- Sharp, A., & Offer, G. (1992). The mechanism of formation of gels from myosin molecules. Journal of Science Food and Agriculture, 58(1), 63–73. https://doi.org/10.1002/jsfa.2740580112
- Shi, F., Li, Y., Wang, L., Yang, Y., Lu, K., Wu, S., & Ming, J. (2018). Measurement of moisture transformation and distribution in Tricholoma matsutake by low field nuclear magnetic resonance during the hot-air drying process. Journal of Food Processing and Preservation, 42(3), e13565.
- Shie, J. S., & Park, J. W. (1999). Physical characteristics of surimi seafood as affected by thermal processing conditions. Journal of Food Science, 64(2), 287–290. https://doi.org/10.1111/j.1365-2621.1999.tb15884.x
- Sun, X. D., & Arntfield, S. D. (2011). Gelation properties of chicken myofibrillar protein induced by transglutaminase cross-linking. Journal of Food Engineering, 107(2), 226–233. https://doi.org/10.1016/j.jfoodeng.2011.06.019
- Tang, C., Wang, S., & Huang, Q. (2012). Improvement of heat-induced fibril assembly of soy β-conglycinin (7S Globulins) at pH 2.0 through electrostatic screening. Food Research International, 46(1), 229–236.
- Tornberg, E. (2005). Effects of heat on meat proteins - Implications on structure and quality of meat products. Meat Science, 70, 493–508. https://doi.org/10.1016/j.meatsci.2004.11.021
- Wołoszyn, J., Wereńska, M., Goluch, Z., Haraf, G., Okruszek, A., Teleszko, M., & Król, B. (2020). The selected goose meat quality traits in relation to various types of heat treatment. Poultry Science, 99(12), 7214–7224. https://doi.org/10.1016/j.psj.2020.09.062
- Wu, M., Xiong, Y. L., Chen, J., Tang, X., & Zhou, G. (2010). Rheological and microstructural properties of porcine myofibrillar protein-lipid emulsion composite gels. Journal of Food Science, 74(4), 207–217. https://doi.org/10.1111/j.1750-3841.2009.01140.x
- Xiong, Y. L., & Brekke, C. J. (1990). Thermal transitions of saltsoluble proteins from pre- and postrigor chicken muscles. Journal of Food Science, 55, 1540.
- Xu, L., Zheng, Y., Zhou, C., Pan, D., Geng, F., Cao, J., & Xia, Q. (2021). Kinetic response of conformational variation of duck liver globular protein to ultrasonic stimulation and its impact on the binding behavior of n-alkenals. LWT - Food Science and Technology, 150, 111890. https://doi.org/10.1016/j.lwt.2021.111890
- Xu, Y., Han, M., Huang, M., & Xu, X. (2021). Enhanced heat stability and antioxidant activity of myofibrillar protein-dextran conjugate by the covalent adduction of polyphenols. Food Chemistry, 352, 129376.
- Zheng, H., Han, M., Bai, Y., Xu, X., & Zhou, G. (2019). Combination of high pressure and heat on the gelation of chicken myofibrillar proteins. Innovative Food Science and Emerging Technologies, 52, 122–130. https://doi.org/10.1016/j.ifset.2018.10.014
- Zhu, C. Z., Jin, H. Q., Yin, F., Cui, W. M., Zhang, Q. H., & Zhao, G. M. (2021). Emulsion-forming properties of heat-induced pork myofibrillar protein affected by NaCl. International Journal of Food Science and Technology, 56, 3016–3025. https://doi.org/10.1111/ijfs.14945