Home Effects of three treatments on protein structure and gel properties of Perccottus glenii myofibrillar protein
Article
Licensed
Unlicensed Requires Authentication

Effects of three treatments on protein structure and gel properties of Perccottus glenii myofibrillar protein

  • Guochuan Jiang , Lili Tian , Ruifeng Hu , Hongrui Sun , Yuan Fu , Wanchun Guo , Xuejun Liu EMAIL logo and Xiaohui Yan EMAIL logo
Published/Copyright: December 6, 2021

Abstract

In order to improve Perccottus glenii myofibrillar protein (MP) gel properties, three treatments were evaluated: ultrasonic, transglutaminase (TGase) and combined ultrasonic-transglutaminase treatments. Combined ultrasonic-transglutaminase treatment altered protein structure and gel properties most dramatically. As compared with untreated control group protein, treated protein gels possessed decreased sulfhydryl group content and increases in water holding capacity, whiteness value and hydrophobic interactions that increased gel strength value by up to 3.79 times that of untreated protein gel. Protein structural and Differential scanning calorimetry (DSC) analyses revealed that combined ultrasonic-TGase treatment increased both protein thermal denaturation temperature and UV absorbance (as compared to control and other treatment groups) that supported formation of MP gels with desirable characteristics. These results provide a theoretical basis for development of superior MP gels to promote greater utilization of this fish protein resource by the food industry.


Corresponding authors: Xuejun Liu, Jilin Agricultural University, Changchun, 130118, China, E-mail: ; and Xiaohui Yan, Jilin Business and Technology College, Changchun, 130507, China, E-mail:

  1. Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.

  2. Research funding: The authors would like to thank the Science and Technology Development Program of Jilin Province (grant no. 20130206061YY) for financial support.

  3. Conflict of interest statement: The authors declare no conflicts of interest regarding this article.

References

1. Sochaya, C, Soottawat, B, Aran, HK. Comparative study on protein cross‐linking and gel enhancing effect of microbial transglutaminase on surimi from different fish. J Sci Food Agric 2012;92:844–52. https://doi.org/10.1002/jsfa.4656.Search in Google Scholar PubMed

2. Tian, LL, Wu, XG, Liu, XJ, Gou, MX, Ren, ZF, Liu, YC. Response surface optimization of conditions for gel preparation of Perccottus glenii myofibril proteins. In Proceedings of the symposium on environment, energy and earth sciences. ICFSE 2016. International Conference on food science and Engineering, Guangzhou, China, 2016. https://doi.org/10.12783/dteees/sses/icfse2016/10677.Search in Google Scholar

3. Macfarlane, JJ, Sehlnidt, GR, Turner, RH. Binding of meat pieces: a comparison of myosin, actomyosin and sarcoplasmic proteins as binding agents. J Food Sci 1977;42:1603–6. https://doi.org/10.1111/j.1365-2621.1977.tb08437.x.Search in Google Scholar

4. Luo, YK, Kuwahara, R, Kaneniwa, M, Murata, Y, Yokoyama, M. Comparison of gel properties of surimi from Alaska pollock and three freshwater fish species: effects of thermal processing and protein concentration. J Food Sci 2001;66:548–54. https://doi.org/10.1111/j.1365-2621.2001.tb04600.x.Search in Google Scholar

5. Zhao, ZR, Wang, SJ, Li, DY, Zhou, YJ. Effect of xanthan gum on the quality of low sodium salted beef and property of myofibril proteins. Food Sci Hum Well 2021;10:112–8. https://doi.org/10.1016/j.fshw.2020.09.003.Search in Google Scholar

6. Li, YQ, Kong, BH, Xia, XF, Liu, Q. Inhibition of frozen storage-induced oxidation and structural changes in myofibril of common carp (Cyprinus carpio) surimi by cryoprotectant and hydrolysed whey protein addition. Int J Food Sci Technol 2013;48:1916–23. https://doi.org/10.1111/ijfs.12171.Search in Google Scholar

7. Villamonte, G, Jury, V, Jung, S, Lamballerie, MD. Influence of xanthan gum on the structural characteristics of myofibrillar proteins treated by high pressure. J Food Sci 2015;80:522–31. https://doi.org/10.1111/1750-3841.12789.Search in Google Scholar PubMed

8. Kang, D, Zhang, W, Lorenzo, JM, Chen, X. Structural and functional modification of food proteins by high power ultrasound and its application in meat processing. Crit Rev Food Sci Nutr 2020;25:1–20. https://doi.org/10.1080/10408398.2020.1767538.Search in Google Scholar PubMed

9. Chemat, F, Zill-e-Huma, Khan, MK. Applications of ultrasound in food technology: processing, preservation and extraction. Ultrason Sonochem 2011;18:813–35. https://doi.org/10.1016/j.ultsonch.2010.11.023.Search in Google Scholar PubMed

10. Alarcon-Rojo, AD, Carrillo-Lopez, LM, Reyes-Villagrana, R, Huerta-Jiménez, M, Garcia-Galicia, IA. Ultrasound and meat quality: a review. Ultrason Sonochem 2019;55:369–82. https://doi.org/10.1016/j.ultsonch.2018.09.016.Search in Google Scholar PubMed

11. Awad, TS, Moharram, HA, Shaltout, OE, Asker, D, Youssef, MM. Applications of ultrasound in analysis, processing and quality control of food: a review. Food Res Int 2012;48:410–27. https://doi.org/10.1016/j.foodres.2012.05.004.Search in Google Scholar

12. Li, K, Kang, ZL, Zou, YF, Xu, XL. Effect of ultrasound treatment on functional properties of reduced-salt chicken breast meat batter. J Food Sci Technol 2015;52:2622–33. https://doi.org/10.1007/s13197-014-1356-0.Search in Google Scholar PubMed PubMed Central

13. Jayasooriya, SD, Torley, PJ, D’Arcy, BR, Bhandari, BR. Effect of high power ultrasound and ageing on the physical properties of bovine semitendinosus and longissimus muscles. Meat Sci 2007;75:628–39. https://doi.org/10.1016/j.meatsci.2006.09.010.Search in Google Scholar PubMed

14. Saleem, R, Ahmad, R. Effect of low frequency ultrasonication on biochemical and structural properties of chicken actomyosin. Food Chem 2016;205:43–51. https://doi.org/10.1016/j.foodchem.2016.03.003.Search in Google Scholar PubMed

15. Fan, D, Huang, L, Li, B, Huang, J, Zhao, J, Yan, B, et al.. Acoustic intensity in ultrasound field and ultrasound-assisted gelling of surimi. LWT – Food Sci Technol 2017;75:497–504. https://doi.org/10.1016/j.lwt.2016.08.002.Search in Google Scholar

16. Ahhmed, AM, Kuroda, R, Kawahara, S, Ohta, K, Nakade, K, Aoki, T, et al.. Dependence of microbial transglutaminase on meat type in myofibrillar proteins cross-linking. Food Chem 2009;112: 354–61. https://doi.org/10.1016/j.foodchem.2008.05.078.Search in Google Scholar

17. Chanarat, S, Benjakul, S. Impact of microbial transglutaminase on gelling properties of Indian mackerel fish protein isolates. Food Chem 2013;136:929–37. https://doi.org/10.1016/j.foodchem.2012.09.021.Search in Google Scholar PubMed

18. Chanarat, S, Benjakul, S, H-Kittikun, A. Comparative study on protein cross‐linking and gel enhancing effect of microbial transglutaminase on surimi from different fish. J Sci Food Agric 2012;92:844–52. https://doi.org/10.1002/jsfa.4656.Search in Google Scholar PubMed

19. Liu, Q, Chen, Q, Kong, B, Han, JC, He, XY. The influence of superchilling and cryoprotectants on protein oxidation and structural changes in the myofibrillar proteins of common carp (Cyprinus carpio) surimi. LWT – Food Sci Technol 2014;57:n603–11. https://doi.org/10.1016/j.lwt.2014.02.023.Search in Google Scholar

20. Park, D, Xiong, YL. Oxidative modification of amino acids in porcine myofibrillar protein isolates exposed to three oxidizing systems. Food Chem 2007;103:607–16. https://doi.org/10.1016/j.foodchem.2006.09.004.Search in Google Scholar

21. Jiang, GC, Wang, LY, Liu, YC, Sun, HR, Zhang, JL, Liu, XJ, et al.. Effect of modification on the structure and gel properties of porcine myofibrillar protein. Food Sci 2019;40:89–95. https://doi.org/10.7506/spkx1002-6630-20181011-088.Search in Google Scholar

22. Salvador, P, Toldrà, M, Saguer, E, Carretero, C, Parés, D. Microstructure-function relationships of heat-induced gels of porcine haemoglobin. Food Hydrocoll 2009;23:1654–9. https://doi.org/10.1016/j.foodhyd.2008.12.003.Search in Google Scholar

23. Xiong, GY, Fu, XY, Pan, DM, Qi, J, Xu, XL, Jiang, XJ. Influence of ultrasound-assisted sodium bicarbonate marination on the curing efficiency of chicken breast meat. Ultrason Sonochem 2020;60:104808. https://doi.org/10.1016/j.ultsonch.2019.104808.Search in Google Scholar

24. Liang, F, Zhu, YJ, Ye, T, Jiang, ST, Lin, L, Lu, JF. Effect of ultrasound assisted treatment and microwave combined with water bath heating on gel properties of surimi-crabmeat mixed gels. LWT – Food Sci Technol 2020;133:110098. https://doi.org/10.1016/j.lwt.2020.110098.Search in Google Scholar

25. Beveridge, T, Toma, SJ, Nakai, S. Determination of SH- and SS-groups in some food proteins using Ellman’s reagent. J Food Sci 1974;39:49–51. https://doi.org/10.1111/j.1365-2621.1974.tb00984.x.Search in Google Scholar

26. Gómez-Guillén, MC, Borderı́as, AJ, Montero, P. Chemical interactions of nonmuscle proteins in the network of Sardine (Sardina pilchardus) muscle gels. LWT – Food Sci Technol 1997;30:602–8. https://doi.org/10.1006/fstl.1997.0239.Search in Google Scholar

27. Rincóna, L, Castro, PL, Álvarez, B, Hernándezc, MD, Álvarez, A, Claret, A, et al.. Differences in proximal and fatty acid profiles, sensory characteristics, texture, color and muscle cellularity between wild and farmed blackspot seabream (Pagellus bogaraveo). Aquaculture 2016;451:195–204. https://doi.org/10.1016/j.aquaculture.2015.09.016.Search in Google Scholar

28. Lange, R, Balny, C. UV-visible derivative spectroscopy under high pressure. Biochim Biophys Acta 2002;1595:80–93. https://doi.org/10.1016/S0167-4838(01)00336-3.Search in Google Scholar

29. Cao, ZM. Effects of three physically-modified pea proteins on the quality of chicken minced meat gel. China: Henan Institute of Science and Technology; 2021.Search in Google Scholar

30. Zhang, C, Li, XA, Wang, H, Xia, X, Kong, B. Ultrasound-assisted immersion freezing reduces the structure and gel property deterioration of myofibrillar protein from chicken breast. Ultrason Sonochem 2020;27. https://doi.org/10.1016/j.ultsonch.2020.105137.Search in Google Scholar PubMed

31. Zhao, YY, Wang, P, Zou, YF, Li, K, Kang, ZL, Xu, XL, et al.. Effect of pre-emulsification of plant lipid treated by pulsed ultrasound on the functional properties of chicken breast myofibrillar protein composite gel. Food Res Int 2014;58:98–104. https://doi.org/10.1016/j.foodres.2014.01.024.Search in Google Scholar

32. Hu, H, Fan, X, Zhou, Z, Xu, XY, Fan, G, Wang, LF, et al.. Acid-induced gelation behavior of soybean protein isolate with high intensity ultrasonic pre-treatments. Ultrason Sonochem 2013;20:187–95. https://doi.org/10.1016/j.ultsonch.2012.07.011.Search in Google Scholar PubMed

33. Wu, H, Ge, M, Zhou, X, Jiang, S, Lin, L, Lu, J. Nutritional qualities of normal and precocious adult male Chinese mitten crabs (Eriocheir sinensis). Aquacult Res 2019;50:2267–75. https://doi.org/10.1111/are.14107.Search in Google Scholar

34. Sun, XD, Arntfield, SD. Gelation properties of myofibrillar/pea protein mixtures induced by transglutaminase crosslinking. Food Hydrocoll 2012;27:394–400. https://doi.org/10.1016/j.foodhyd.2011.11.001.Search in Google Scholar

35. Madadlou, A, Emam-Djomeh, Z, Mousavi, ME, Mohamadifar, M, Ehsani, M. Acid-induced gelation behavior of sonicated casein solutions. Ultrason Sonochem 2010;17:153–8. https://doi.org/10.1016/j.ultsonch.2009.06.009.Search in Google Scholar PubMed

36. Cao, C, Xiao, Z, Tong, H, Tao, X, Gu, D, Wu, Y, et al.. Effect of ultrasound-assisted enzyme treatment on the quality of chicken breast meat. Food Bioprod Process 2021;125:193–203. https://doi.org/10.1016/j.fbp.2020.11.005.Search in Google Scholar

37. Chen, H, Kong, B, Guo, Y, Xia, X, Diao, X, Li, P. The effectiveness of cryoprotectants in inhibiting multiple freeze-thaw-induced functional and rheological changes in the myofibrillar proteins of common carp (Cyprinus carpio) surimi. Food Biophys 2013;8:302–10. https://doi.org/10.1007/s11483-013-9305-4.Search in Google Scholar

38. Puolanne, E, Halonen, M. Theoretical aspects of water-holding in meat. Meat Sci 2010;86:151–65. https://doi.org/10.1016/j.meatsci.2010.04.038.Search in Google Scholar PubMed

39. Ionescu, A, Aprodu, I, Daraba, A, Porneala, L. The effects of transglutaminase on the functional properties of myofibrillar protein concentrate obtained from beef heart. Meat Sci 2008;79:278–84. https://doi.org/10.1016/j.meatsci.2007.09.011.Search in Google Scholar PubMed

40. Li, K, Kang, ZL, Zhao, YY, Xu, XL, Zhou, GH. Use of high-intensity ultrasound to improve functional properties of batter suspensions prepared from PSE-like chicken breast meat. Food Bioprocess Technol 2014;7:3466–77. https://doi.org/10.1007/s11947-014-1358-y.Search in Google Scholar

41. Zhang, Z, Yang, Y, Tang, X, Chen, Y, You, Y. Chemical forces and water holding capacity study of heat-induced myofibrillar protein gel as affected by high pressure. Food Chem 2015;188:111–8. https://doi.org/10.1016/j.foodchem.2015.04.129.Search in Google Scholar PubMed

42. Dan, J, Huang, Q, Xiong, S. Chemical interactions and gel properties of black carp actomyosin affected by MTGase and their relationships. Food Chem 2016;196:1180–7. https://doi.org/10.1016/j.foodchem.2015.10.030.Search in Google Scholar PubMed

43. Zhang, Z, Regenstein, JM, Zhou, P, Yang, Y. Effects of high intensity ultrasound modification on physicochemical property and water in myofibrillar protein gel. Ultrason Sonochem 2017;34:960–7. https://doi.org/10.1016/j.ultsonch.2016.08.008.Search in Google Scholar PubMed

44. Westphalen, AD, Briggs, JL, Lonergan, SM. Influence of muscle type on rheological properties of porcine myofibrillar protein during heat-induced gelation. Meat Sci 2006;72:697–703. https://doi.org/10.1016/j.meatsci.2005.09.021.Search in Google Scholar PubMed

45. Aktas, N, Kilic, B. Effect of microbial transglutaminase on thermal and electrophoretic properties of ground beef. LWT – Food Sci Technol 2005;38:815–9. https://doi.org/10.1016/j.lwt.2004.10.003.Search in Google Scholar

Received: 2021-06-21
Accepted: 2021-11-07
Published Online: 2021-12-06

© 2021 Walter de Gruyter GmbH, Berlin/Boston

Downloaded on 29.9.2025 from https://www.degruyterbrill.com/document/doi/10.1515/ijfe-2021-0190/html
Scroll to top button