Skip to main content

Advertisement

Log in

Myofibrillar Protein Structure and Gel Properties of Trichiurus Haumela Surimi Subjected to High Pressure or High Pressure Synergistic Heat

  • Original Paper
  • Published:
Food and Bioprocess Technology Aims and scope Submit manuscript

Abstract

The changes in gel properties and myofibrillar protein structure of Trichiurus haumela surimi subjected to high pressure (300–450 MPa; 5 min) or high pressure synergistic heat (90 °C; 30 min) treatment were investigated. The results showed that high pressure below 400 MPa could improve the gel properties. The water holding capacity of the 350 MPa group increased by 27.40% compared with the control group. Moreover, the gel strength of surimi gel induced by high pressure of 300 MPa and 350 MPa increased by 38.08% and 40.00%, respectively, and continually increased by 17.86% and 21.00% after further heating. Both of high pressure and heating affected the composition of myofibrillar protein and partially degraded the actin and myosin heavy chain. High pressure reduced the contents of α-helix and β-turn, but increased β-sheet and random coil in the myofibrillar protein. Subsequent heat treatment converted the partial β-sheet into the α-helix structure. In addition, in the gels of surimi subjected to high pressure, the secondary structure of myofibrillar protein was significantly correlated with the whiteness, gel strength, and texture characteristics of the gels. Collectively, the results supported an optimum pressure of 300–350 MPa for the induction of hairtail surimi gel.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5

Similar content being viewed by others

References

  • Barrera, A. M., Ramírez, J. A., González-Cabriales, J. J., & Vázquez, M. (2002). Effect of pectins on the gelling properties of surimi from silver carp. Food Hydrocolloids, 16, 441–447.

    Article  CAS  Google Scholar 

  • Buamard, N., & Benjakul, S. (2018). Combination effect of high pressure treatment and ethanolic extract from coconut husk on gel properties of sardine surimi. LWT - Food Science and Technology, 91, 361–367.

    Article  CAS  Google Scholar 

  • Cando, D., Herranz, B., Borderías, A., & Moreno, H. (2015). Effect of high pressure on reduced sodium chloride surimi gels. Food Hydrocolloids, 51, 176–187.

    Article  CAS  Google Scholar 

  • Cando, D., Moreno, H. M., Borderas, A. J., & Skara, T. (2016). Combined effect of high hydrostatic pressure and lysine or cystine addition in low-grade surimi gelation with low salt content. Food and Bioprocess Technology, 9(8), 1391–1398.

    Article  CAS  Google Scholar 

  • Chakraborty, T., Jayaprakash, S., Srinivasu, P., Madhavendra, S., Ravi, S. A., & Kunwar, A. (2002). Furanoid sugar amino acid based peptidomimetics: well-defined solution conformations to gel-like structures. Tetrahedron, 58(14), 2853–2859.

    Article  CAS  Google Scholar 

  • Cheng, Z. Z., Yang, R. J., & Zhao, W. (2011). Gel properties of ribbonfish (Trichiurus haumela) surimi gels with soybean dietary fiber induced by high pressure and heating. International Journal of Food Engineering, 7(6), 39–47.

    Google Scholar 

  • Fernández-Martín, F., Pérez-Mateos, M., & Montero, P. (1998). Effect of pressure/heat combinations on blue whiting (Micromesistius poutassou) washed mince: thermal and mechanical properties. Journal of Agricultural and Food Chemistry, 46(8), 3257–3264.

    Article  Google Scholar 

  • Greenfield, N. J. (2007). Using circular dichroism spectra to estimate protein secondary structure. Nature Protocols, 1(6), 2876–2890.

    Article  CAS  Google Scholar 

  • Guo, Z. B., Li, Z. Y., Wang, J. Y., & Zheng, B. D. (2019). Gelation properties and thermal gelling mechanism of golden threadfin bream myosin containing CaCl2 induced by high pressure processing. Food Hydrocolloids, 95, 43–52.

    Article  CAS  Google Scholar 

  • Imtiaz-Ul-Islam, M., Hong, L., & Langrish, T. (2011). CO2 capture using whey protein isolate. Chemical Engineering Journal, 171(3), 1069–1081.

    Article  CAS  Google Scholar 

  • Jin, S. K., Kim, I. S., Jung, H. J., Kim, D. H., Choi, Y. J., & Hur, S. J. (2011). Effect of cryoprotectants on chemical, mechanical and sensorial characteristics of spent laying hen surimi. Food and Bioprocess Technology, 4(8), 1407–1413.

    Article  CAS  Google Scholar 

  • Kaewudom, P., Benjakul, S., & Kijroongrojana, K. (2013). Properties of surimi gel as influenced by fish gelatin and microbial transglutaminase. Food Bioscience, 1, 39–47.

    Article  CAS  Google Scholar 

  • Kudre, T. G., & Benjakul, S. (2014). Effects of bambara groundnut protein isolates and microbial transglutaminase on textural and sensorial properties of surmi gel from sardine (Sardinella albella). Food and Bioprocess Technology, 7(6), 1570–1580.

    Article  CAS  Google Scholar 

  • Lanier, T. C. (1996). Gelation of surimi pastes treated by high isostatic pressure. Progress in Biotechnology, 13(C), 357–362.

    CAS  Google Scholar 

  • Le, X. T., & Turgeon, S. L. (2015). Textural and waterbinding behaviors of β-lactoglobulin-xanthan gum electrostatic hydrogels in relation to their microstructure. Food Hydrocolloids, 49, 216–223.

    Article  CAS  Google Scholar 

  • Li, W., Bai, Y., Mousaa, S. A. S., Zhang, Q., & Shen, Q. (2012). Effect of high hydrostatic pressure on physicochemical and structural properties of rice starch. Food and Bioprocess Technology, 5(6), 2233–2241.

    Article  CAS  Google Scholar 

  • Li, G., Chen, Y., Xuan, S., Lv, M., Zhang, J., Lou, Q., Jia, R., & Yang, W. (2019). Rheological properties and structure of myofibrillar protein extracted from Oratosquilla oratoria muscle as affected by ultra-high pressure. International Journal of Food Properties, 22(1), 1310–1321.

    Article  CAS  Google Scholar 

  • Liu, R., Zhao, S. M., Xiong, S. B., Xie, B. J., & Qin, L. H. (2008). Role of secondary structures in the gelation of porcine myosin at different pH values. Meat Science, 80(3), 632–639.

    Article  CAS  Google Scholar 

  • Lv, M. C., Mei, K. L., Zhang, H., Xu, D. L., & Yang, W. G. (2018). Effects of electron beam irradiation on the biochemical properties and structure of myofibrillar protein from Tegillarca granosa meat. Food Chemistry, 254, 64–69.

    Article  CAS  Google Scholar 

  • Ma, X. S., Yi, S. M., Yu, Y. M., Li, J. R., & Chen, J. R. (2015). Changes in gel properties and water properties of Nemipterus virgatus surimi gel induced by high-pressure processing. LWT - Food Science and Technology, 61(2), 377–384.

    Article  CAS  Google Scholar 

  • Moreno, H. M., Cardoso, C., Solas, M. T., & Borderías, A. J. (2009). Improvement of cold and thermally induced gelation of giant squid (Dosidicus gigas) surimi. Journal of Aquatic Food Product Technology, 18(4), 312–330.

    Article  CAS  Google Scholar 

  • Moreno, H. M., Bargiela, V., Tovar, C. A., Cando, D., Borderias, A. J., & Herranz, B. (2015). High pressure applied to frozen flying fish (Parexocoetus brachyterus) surimi: Effect on physicochemical and rheological properties of gels. Food Hydrocolloids, 48, 127–134.

    Article  CAS  Google Scholar 

  • Nagano, T., & Tokita, M. (2011). Viscoelastic properties and microstructures of 11S globulin and soybean protein isolate gels: magnesium chloride-induced gels. Food Hydrocolloids, 25(7), 1647–1654.

    Article  CAS  Google Scholar 

  • Petcharat, T., & Benjakul, S. (2018). Effect of gellan incorporation on gel properties of bigeye snapper surimi. Food Hydrocolloids, 77, 746–753.

    Article  CAS  Google Scholar 

  • Qiu, C. J., Xia, W. S., & Jiang, Q. X. (2013). Effect of high hydrostatic pressure (HHP) on myofibril-bound serine proteinases and myofibrillar protein in silver carp (Hypophthalmichthys molitrix). Food Research International, 52(1), 199–205.

    Article  CAS  Google Scholar 

  • 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.

    Article  CAS  Google Scholar 

  • Wang, B. W., & Xiong, Y. L. (1998). Evidence of proteolytic activity and its effect on gelation of myofibrillar protein concentrate from bovine cardiac muscle. Journal of Agricultural and Food Chemistry, 46(8), 3054–3059.

    Article  CAS  Google Scholar 

  • Wang, J. Y., Li, Z. Y., Zheng, B. D., Zhang, Y., & Guo, Z. B. (2019). Effect of ultra-high pressure on the structure and gelling properties of low salt golden threadfin bream (Nemipterus virgatus) myosin. LWT - Food Science and Technology, 100, 381–390.

    Article  CAS  Google Scholar 

  • Xiong, G. Q., Cheng, W., Ye, L. X., Du, X., Zhou, M., Lin, R. T., et al. (2009). Effects of konjac glucomannan on physicochemical properties of myofibrillar protein and surimi gels from grass carp (Ctenopharyngodon idella). Food Chemistry, 116(2), 413–418.

    Article  CAS  Google Scholar 

  • Xu, X. L., Han, M. Y., Fei, Y., & Zhou, G. H. (2011). Raman spectroscopic study of heat-induced gelation of pork myofibrillar proteins and its relationship with textural characteristic. Meat Science, 87(3), 159–164.

    Article  CAS  Google Scholar 

  • Yang, J. T., Wu, C.-S. C., & Martinez, H. M. (1986). Calculation of protein conformation from circular dichroism. Methods in Enzymology, 130, 208–269.

    Article  CAS  Google Scholar 

  • Zhang, T., Xue, Y., Li, Z., Wang, Y., Yang, W., & Xue, C. (2014). Effects of ozone-induced oxidation on the physicochemical properties of myofibrillar proteins recovered from bighead carp (Hypophthalmichthys nobilis). Food and Bioprocess Technology, 8(1), 181–190.

    Article  CAS  Google Scholar 

  • Zhang, Z. Y., Yang, Y. L., Tang, X. Z., Chen, Y. J., & You, Y. (2015). Chemical forces and water holding capacity study of heat-induced myofibrillar protein gel as affected by high pressure. Food Chemistry, 188, 111–118.

    Article  CAS  Google Scholar 

  • Zhang, H., Wang, W., Zhang, S., Wang, H., & Ye, Q. (2016). Influence of 10-MeV E-beam irradiation and vacuum packaging on the shelf-life of grass carp surimi. Food and Bioprocess Technology, 9(5), 830–838.

    Article  CAS  Google Scholar 

  • Zhang, L., Li, Q., Shi, J., Zhu, B., & Luo, Y. (2018). Changes in chemical interactions and gel properties of heat-induced surimi gels from silver carp (Hypophthalmichthys molitrix) fillets during setting and heating: effects of different washing solutions. Food Hydrocolloids, 75, 116–124.

    Article  CAS  Google Scholar 

  • Zhou, H., Wang, C., Ye, J., Tao, R., Chen, H., & Cao, F. (2016). Effects of enzymatic hydrolysis assisted by high hydrostatic pressure processing on the hydrolysis and allergenicity of proteins from ginkgo seeds. Food and Bioprocess Technology, 9(5), 839–848.

    Article  CAS  Google Scholar 

Download references

Funding

This work was supported by the National Key Research and Development Program of China [2018YFD0901105], the Public Welfare Technology Research Project of Zhejiang Province [LGN18C200020], was sponsored by K. C. Wong Magna Fund in Ningbo University.

Author information

Authors and Affiliations

Authors

Corresponding authors

Correspondence to Ru Jia or Wenge Yang.

Ethics declarations

Conflict of Interest

The authors declare that they have no conflict of interest.

Additional information

Publisher’s Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Chen, Y., Xu, A., Yang, R. et al. Myofibrillar Protein Structure and Gel Properties of Trichiurus Haumela Surimi Subjected to High Pressure or High Pressure Synergistic Heat. Food Bioprocess Technol 13, 589–598 (2020). https://doi.org/10.1007/s11947-020-02416-x

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11947-020-02416-x

Keywords

Navigation