Determination of collagen and pH measurement in beef: Modern laboratory techniques

Year 2024, , 126 - 130, 31.08.2024

Sedef Keleş , Nezir Yaşar Toker

https://doi.org/10.30704/http-www-jivs-net.1479918

Abstract

Determining the pH value and collagen value in beef is very important in terms of healthy and quality nutrition. Collagen value is of great importance in meat-like products in order to offer healthy products to consumers. Today, various measurement techniques are used to measure pH value and collagen value. However, the success and reliability of each measurement varies. Therefore, more sensitive and reliable measurement methods need to be developed. Within the scope of this study, modern techniques used in the food industry to measure the pH value and collagen value of cut meat were examined. The reliability and acceptance level of each technique varies. This research aims to contribute to the development of more accurate methods for measuring collagen and pH values. In this way, it is aimed to increase the quality of beef products and offer healthier and more delicious products to consumers.

Keywords

pH, Beef, Collagen, Measurement and Techniques

References

• Ankaralıgil, P., & Güneşer, B. (2021) Importance of Instrumental Analysis Techniques in Determination of Functional Food Components. European Journal of Science and Technology, 28, 251-258.
• Ariffin, N., Hasham, R. (2020) Assessment of non-invasive techniques and herbal-based products on dermatological physiology and intercellular lipid properties. Heliyon, 6(5): e03955.
• Blanco, M., Jurie, C., Micol, D., Agabriel, J., Picard, B., & Garcia-Launay, F. (2013). Impact of animal and management factors on collagen characteristics in beef: a meta-analysis approach. Animal, 7(7), 1208-1218.
• Bruce, H., & Roy, B. (2009) Production factors affecting the contribution of collagen to beef toughness. Journal of Animal Science, 97(5), 2270-2278.
• Diesner, S. C., Bergmayr, C., Pfitzner, B., Assmann, V., Krishnamuthy, D., Starkl, P., Endesfelder, D., Rothballer, M., Welzl, G., Rattei, T., Eiwegger, T., Szépfalusi, Z., Fehrenbach, H., Jensen-Jarolim, E., Hartmann, A., Pali-Schöll, I., & Untersmayr, E. (2016) A distinct microbiota composition is associated with protection from food allergy in an oral mouse immunization model. Clinical Immunology, 173, 10-18.
• Farmer, L., & Farrell, D. (2018). Review: beef-eating quality: a european journey. Animal,12(11), 2424-2433. Food and Agriculture Organization of the United Nations (1998). FAO Production Yearbook (p.233). Rome, Italy.
• Fratzl, P. (2008). Collagen: structure and mechanics, an introduction. In Collagen: structure and mechanics (pp. 1-13). Boston, MA: Springer US.
• Geletu, U. S., Usmael, M. A., Mummed, Y. Y., & Ibrahim, A. M. (2021). Quality of cattle meat and its compositional constituents. Veterinary Medicine International, 1-9
• Gómez, I., Beriain, M., Sarriés, M., Insausti, K., & Mendizabal, J. (2014). Low-fat beef patties with augmented omega-3 fatty acid and cla levels and influence of grape seed extract. Journal of Food Science, 79(11), S2368-S2376. Hills, A. E. (2017). Spectroscopy in biotechnology research and development. Encyclopedia of Spectroscopy and Spectrometry, 198-202. Holmes, D. F., Lu, Y., Starborg, T., & Kadler, K. E. (2018). Collagen fibril assembly and function. Current Topics in Developmental Biology, 130, 107-142.
• Karoui, R., & Blecker, C. (2011). Fluorescence spectroscopy measurement for quality assessment of food systems-a review. Food and Bioprocess Technology, 4, 364-386.
• Lucarini, M, Durazzo, A, Del Pulgar, J. S., Gabrielli, P, & Lombardi-Boccia, G. (2018). Determination of fatty acid content in meat and meat products: The FTIR-ATR approach. Food Chemistry, 267, 223-230.
• Matinong, A. M. E., Chisti, Y., Pickering, K. L., & Haverkamp, R. G. (2022). Collagen extraction from animal skin. Biology, 11(6), 905.
• Messia, M. C., Di Falco, T., Panfili, G., & Marconi, E. (2008). Rapid determination of collagen in meat-based foods by microwave hydrolysis of proteins and HPAEC–PAD analysis of 4-hydroxyproline. Meat Science, 80(2), 401-409.
• Modzelewska‐Kapituła, M., Nogalski, Z., & Kwiatkowska, A. (2016). The influence of crossbreeding on collagen solubility and tenderness of Infraspinatus and Semimembranosus muscles of semi‐intensively reared young bulls. Animal Science Journal, 87(10), 1312-1321.
• Monago-Maraña, O., Wold, J. P., Rødbotten, R., Dankel, K. R., & Afseth, N. K. (2021). Raman, near-infrared and fluorescence spectroscopy for determination of collagen content in ground meat and poultry by-products. Lwt, 140, 110592.
• Oh, E., Lee, B., & Choi, Y. (2019). Associations of heat-shock protein expression with meat quality and sensory quality characteristics in highly marbled longissimus thoracis muscle from hanwoo steers categorized by warner-bratzler shear force value. Foods, 8(12), 638.
• Rahman, M., Hossain, M., Rahman, S., Amin, M., & Oh, D. (2015). Evaluation of physicochemical deterioration and lipid oxidation of beef muscle affected by freeze-thaw cycles. Korean Journal for Food Science of Animal Resources, 35(6), 772-782.
• Sheppard, A. J., & O'Dell, R. G. (2003). Cholesterol properties and determination. Encyclopedia of Food Sciences and Nutrition, 1220-1226.
• Sherman, V. R., Yang, W., & Meyers, M. A. (2015). The materials science of collagen. Journal of the mechanical behavior of biomedical materials, 52, 22-50.
• Shockcor, J. P. (2017). Hplc-nmr, pharmaceutical applications. Encyclopedia of Spectroscopy and Spectrometry, 141-151.
• Sorushanova, A., Skoufos, I., Tzora, A., Mullen, A. M., & Zeugolis, D. I. (2021). The influence of animal species, gender and tissue on the structural, biophysical, biochemical and biological properties of collagen sponges. Journal of Materials Science: Materials in Medicine, 32, 1-12.
• Szałkowska, A., & Modzelewska-Kapituła, M. (2017). Collagen profile and tenderness of strip loin and silverside originated from Polish Holstein-Friesian bulls of the black and white variety. Acta Alimentaria, 46(3), 378-383.
• Şireli, H. D. (2018). Traditional methods and new techniques used in determining meat quality in carcasses. Journal of Dicle University Institute of Science and Technology, 7(3), 126-132.
• Warner, R. D., Dunshea, F. R., Gutzke, D., Lau, J., & Kearney, G. (2014). Factors influencing the incidence of high rigor temperature in beef carcasses in Australia. Animal Production Science, 54(4), 363-374.
• Weston, A. R., Rogers, R. W., & Althen, T. G. (2002). The role of collagen in meat tenderness. The Professional Animal Scientist, 18(2), 107-111.
• Zarkadas, C. G., & Maloney, S. A. (1998). Assessment of the protein quality of the smooth muscle myofibrillar and connective tissue proteins of chicken gizzard. Poultry Science, 77(5), 770-779.