High pressure treatment and the effects on meat proteins

Main Article Content

Vibeke Orlien http://orcid.org/0000-0003-4354-6591

Abstract

High pressure (HP) has the prospect to engineer protein conformation, but the fundamentals of physicochemical HP-effects on biomolecules need to be addressed before HP can be fully exploited.

When understanding the mechanisms of HP-induced changes, HP can be used in targeted and unique biomolecule architecture. Thereby, HP offers opportunities to modify structure and interactions within or between biopolymers. This review introduces the principle of HP and its characteristic followed by a description of the pressure effects on meat proteins. Overall, meat protein systems and meat proteins as such are rather pressure-labile of nature. It is shown that HP results in significant changes in the sarcomere and is capable of modifying meat proteins by pressure-induced changes of the molecular structure. Pressurization (200-800 MPa) of meat affects the structure and functionality of myofibrillar proteins resulting in a considerably decreased solubility due to formation of insoluble aggregates. The underlying mechanisms of these pressure-induced molecular changes consist of two overall steps: 1) rupture of the noncovalent, intermolecular interactions resulting in protein denaturation and 2) formation of new intra- and/or intermolecular non-covalent bonds resulting in aggregation.  How these findings may be useful for future research in medical and pharmaceutical applications is speculated upon.

Article Details

How to Cite
ORLIEN, Vibeke. High pressure treatment and the effects on meat proteins. Medical Research Archives, [S.l.], v. 5, n. 8, aug. 2017. ISSN 2375-1924. Available at: <https://esmed.org/MRA/mra/article/view/1426>. Date accessed: 28 mar. 2024.
Keywords
High pressure, meat proteins, myofibrillar proteins
Section
Review Articles

References

Aertsen, A., Meersman, F., Hendrickx, M.E.G., Vogel, R.F., Michiels, C.W., 2009. Biotechnology under high pressure: applications and implications. Trends in Biotechnology 27 (7), 434-441.

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, 92-99.

Bajovic, B., Bolumar, T., Heinz, V., 2012. Quality considerations with high pressure processing of fresh and value added meat products. Meat Science 92 280-289.

Barba, F. J., Ahrné, L., Xanthakis, E., Landerslev, M. G., Orlien, V., 2017a. Chapter 2. Innovative Technologies. In F. J. Barba, A. Sant´Ana, V. Orlien & M. Koubaa (Ed.), Innovative Technologies for Food Preservation. Inactivation of Spoilage and Pathogenic Microorganisms. 1st Edition. ISBN: 9780128110317. Academic Press: Elsevier

Barba, F. J., Koubaa, M., do Prado-Silva, L., Orlien, V., de Souza Sant’Ana, A., 2017b. Mild processing applied to the inactivation of the main foodborne bacterial pathogens: A review. Trends in Food Science and Technology 66, 20-35.

Boonyaratanakornkit, B.B., Park, C.B., Clark, D.S., 2002. Pressure effects on intra- and intermolecular interactions within proteins. Biochimica et Biophysica Acta 1595, 235-249.

Buckow, R., Sikes, A., Tume, R., 2013. Effect of high pressure on physicochemical properties of meat. Critical Reviews I. Food Science and Nutrition 53, 770-786.

Chan, J.T.Y., Omana, D.A., Betti, M., 2011. Application of high pressure processing to improve the functional properties of pale, soft, and exudative (PSE)-like turkey meat. Innovative Food Science and Emerging Technologies 12, 216-225.

Chapleau, N.J., Lamballerie-Anton, M.I.D., 2003. Changes in myofibrillar proteins interactions and rheological properties induced by high-pressure processing. European Food Research and Technology 216, 470-476.

Chura-Chambi, R.M., Cordeiro, Y., Malavasi, N.V., Lemke, L.S., Rodriques, D., Morganti, L., 2013. An analysis of the factors that affect the dissociation of inclusion bodies and the refolding of endostatin under high pressure. Process Biochemistry 48, 250-259.
Colmenero, F.J., 2002. Muscle protein gelation by combined use of high pressure/temperature. Trends in Food Science & Technology 13, 22-30.

Gollwitzer, H., Mittelmeier, W., Brendle, M., Weber, P., Miethke, T., Hofmann, G.O., Gerdesmeyer, L., Schauwecker, J., Diehl, P., 2009. High Hydrostatic Pressure for Dissinfection of Bone Grafts and Biomaterials: An Experimental Study. The Open Orthopaedics Journal 3, 1-7.

Grossi, A., Gkarane, V., Otte, J.A., Ertbjerg, P., Orlien, V., 2012a. High pressure treatment of brine enhanced pork affects endopeptidase activity, protein solubility, and peptide formation. Food Chemistry 134, 1556-1563.

Grossi, A., Søltoft-Jensen, J., Knudsen, J.C., Christensen, M., Orlien, V., 2012b. Reduction of salt in pork sausages by the addition of carrot fibre or potato starch and high pressure treatment. Meat Science 92, 481-489.

Grossi, A., Olsen, K., Bolumar, T., Rinnan, Å., Øgendahl, L.H., Orlien, V., 2016. The effect of high pressure on the functional properties of pork myofibrillar proteins. Food Chemistry 196, 1005-1015.

Hite, B.H., 1899. The effects of pressure in the preservation of milk. Bulletin West Virginia University Agricultural Experiment Station 58, 15-35.

Iwasaki, T., Noshiroya, K., Saitoh, N., Okano, K., Yamamoto, K., 2006. Studies of the effect of hydrostatic pressure pretreatment on thermal gelation of chicken myofibrils and pork meat patty. Food Chemistry 95, 474-483.

Iwasaki, T., Yamamoto, K., 2003. Changes in rabbit skeletal myosin and its subfragments under high hydrostatic pressure. International Journal of Biological Macromolecules 33, 215-220.

Jung, S., de Lamballerie-Anton, M., Ghoul, M., 2000. Modifications of Ultrastructure and Myofibrillar Proteins of Post-rigor Beef Treated by High Pressure. Lebensmittel -Wissenschaft
Und –Technologie 33, 313-319.

Lee, E.-J., Kim, Y.-J., Lee, N.-H., Hong, S.-I., Yamamoto, K., 2007. Differences in properties of myofibrillar proteins from bovine semitendinosus muscle after hydrostatic pressure or heat treatment. Journal of the Science of Food and Agriculture 87, 40-46.

Lown, D. A., Thirsk, H. R., Lord Wynne-Jones., 1968. Effect of Pressure on Ionization Equilibria in Water at 25 °C. Transactions of the Faraday Society 64 (3), 2073-2080.

Ma, H.-J., Ledward, D.A., 2013. High pressure processing of fresh meat. Meat Science 95, 897-903.

Marcos, B., Mullen, S.M., 2014. High pressure induced changes in beef muscle proteome: Correlation with quality parameters. Meat Science 97, 11-20.

Marshall, W. L., Franck, E. U., 1981. Ion Product of Water Substance, 0-1000 °C, 1-10,000 Bars New International Formulation and Its Background. Journal of Physical and Chemical Reference Data 10 (2), 295-304.

Murchie, L.W., Cruz-Romero, M., Kerry, J.P., Linton, M., Patterson, M.F, Smiddy, M., Kelly, A.L., 2005. High pressure processing of shellfish: A review of microbiological and other quality aspects. Innovative Food Science and Emerging Technologies 6, 257-270.

Olsen, K., Jespersen, B.B., Orlien, V., 2015. Changes of pH in 𝛽-Lactoglobulin and 𝛽-Casein Solutions during High Pressure Treatment. Hindawi Publishing Corporation. Journal of Spectroscopy, 2015, Open access.

Olsen, K. & Orlien, V. (2016) Chapter 11 High pressure processing for modification of food biopolymers. In: Knoerzer, K., Juliano, P., and Smithers, G. ed. Innovative Food Processing Techniques. Cambridge; Woodhead Publishing Limited.

Orlien,V., Olsen, K., Skibsted, L.H., 2007. In situ measurements of pH changes in β-lactoglobulin solutions under high hydrostatic pressure. Journal of Agricultural and Food Chemistry 55(11), 4422-4428.

Rivalain, N., Roquain, J., Demazeau, G., 2010. Development of high hydrostatic pressure in biosciences: Pressure effect on biological structures and potential applications in Biotechnologies. Biotechnology Advances 28, 659–672.

Rusman, H., Gerelt, B., Yamamoto, S., Nishiumi, T., Suzuki, A., 2007. Combined Effects of High Pressure and Heat on Shear Value and Histological Characteristics of Bovine Skeletal Muscle. Asian-Australasian Journal of Animal Sciences 20(6), 994-1001.

Silva, J.L., Foguel, D., Royer, C.A., 2001. Pressure provides new insights into protein folding, dynamics and structure. TRENDS in Biochemical Sciences 26 (10), 612-618.

Simonin, H., Duranton, F., Lamballerie, M.D., 2012. New insights into the high-pressure processing of meat and meat products. Comprehensive Reviews in Food Science and Food Safety 11, 285-306.

Speroni, F., Szerman, N., Vaudagna, S.R., 2014. High hydrostatic pressure processing of beef patties: effects of pressure level and sodium tripolyphosphate and sodium chloride concentrations on thermal and aggregative properties of proteins. Innovative Food Science and Emerging Technologies 23, 10-17.

Steinhauser, E., Diehl, P., Hadaller, M., Schauwecker, J., Busch, R., Gradinger, R., Mittelmeier, W., 2006. Biochemical Investigation of the Effect of High Hydrostatic Pressure Treatment on the Mechanical Properties of Human Bone. Journal of Biomedical Materials Research Part B: Applied Biomaterials 76(1), 130-135.

Sun, X.D., Holley, R.A., 2009. High hydrostatic pressure effects on the texture of meat and meat products. Concise Reviews and Hypotheses in Food Science 75 (1), 17-23.

Suzuki, A., Watanabe, M., Iwamura, K., Ikeuchi, Y., Saito, M., 1990. Effect of high pressure treatment on the ultrastructure and myofibrillar protein of beef skeletal muscle. Agricultural and Biological Chemistry 54 (12), 3085-3091.

Tintchev, F., Bindrich, U., Toepfl, S., Strijowski, U., Heinz, V., Knorr, D., 2013. High hydrostatic pressure/temperature modeling of frankfurter batters. Meat Science 94, 376-387.

Yamamoto, K., Hayashi, S., Yasui, T., 1993. Hydrostatic pressure-induced aggregation of myosin molecules in 0.5 M KCl at pH 6.0. Bioscience, Biotechnology, and Biochemistry 57 (3), 383-389.