Abstract

Meat quality largely depends on the maturation conditions and natural biochemical processes that affect its taste, aroma, tenderness, and technological properties. Dry maturation and technological processing attract a lot of scientific attention. The research objective was to study the effect of dry maturation time on the physicochemical parameters of high-quality beef, as well as the effect of a new curing mix on the properties of raw materials.
The research featured dorsal-lumbar cuts of high-quality beef on maturation days 21 and 40. Matured meat was tested for the main components, the solubility of sarcoplasmic and myofibrillar proteins, the hydrophobicity of myofibrillar proteins, protein oxidation products, and the activity of catalase and peroxidase. The chemical composition was evaluated depending on the dry maturation time using the arbitration method. The solubility of proteins was determined by the calorimetric method with a biuret reagent. The hydrophobicity of myofibrillar proteins was determined by bromophenol blue reaction, and the activity of catalase and peroxidase was determined by standard methods. Proteins were extracted with potassium phosphate buffer (pH 7.2), while myofibrillar proteins were extracted with Tris-HCl and KCl buffers at pH 7.5 and 7.0.
The meat samples were deboned and salted using sodium chloride and a combined mix of 70% magnesium chloride and 30% sodium chloride. The solubility of myofibrillar proteins on day 21 increased by 23.95% but decreased by 14.1% by day 40. The solubility of sarcoplasmic proteins decreased continuously (22.10 and 31.12%, respectively). The obtained data matched the hydrophobicity of proteins. Dry maturation initiated protein oxidation, as demonstrated by carbonyl and sulfhydryl groups of myofibrillar proteins on maturation day 40 (27.85 nmol/L and 27.3 µmol/g of protein, respectively). Sodium chloride and its mix increased the extractability of proteins by 5.2 and 6.9% on day 21 and by 6.8 and 10.6% on day 40 but triggered protein oxidation.
Muscle proteins of high-quality beef proved functional after 21 days of dry maturation. The new mix with reduced sodium content can be recommended for high-quality dry-aged beef production.

Keywords

Meet, dry maturation, ionic strength, protein oxidation, curing mixture, muscle proteins, solubility

REFERENCES

1. Lee HJ, Yoon JW, Kim M, Oh H, Yoon Y, Jo C. Changes in microbial composition on the crust by different air flow velocities and their effect on sensory properties of dry-aged beef. Meat Science. 2019;153:152–158. https://doi.org/10.1016/j.meatsci.2019.03.019
2. Kim J-H, Kim T-K, Shin D-M, Kim H-W, Kim Y-B, Choi Y-S. Comparative effects of dry-aging and wet-aging on physicochemical properties and digestibility of Hanwoo beef. Asian-Australasian Journal of Animal Sciences. 2020;33(3):501–505. https://doi.org/10.5713/ajas.19.0031
3. Kozyrev IV, Mittelshtein TM, Pchelkina VA, Kuznetsova TG, Lisitsyn AB. Marbled beef quality grades under various ageing conditions. Foods and Raw Materials. 2018;6(2):429–437. https://doi.org/10.21603/2308-4057-2018-2-429-437
4. Berger J, Kim YHB, Legako JF, Martini S, Lee J, Ebner P, et al. Dry-aging improves meat quality attributes of grass-fed beef loins. Meat Science.2018;145:285–291. https://doi.org/10.1016/j.meatsci.2018.07.004
5. Kim M, Choe J, Lee HJ, Yoon Y, Yoon S, Jo C. Effects of aging and aging method on physicochemical and sensory traits of different beef cuts. Food Science of Animal Resources. 2019;39(1):54–64. https://doi.org/10.5851/kosfa.2019.e3
6. Hulánková R, Kameník J, Saláková A, Závodský D, Borilova G. The effect of dry aging on instrumental, chemical and microbiological parameters of organic beef loin muscle. LWT – Food Science and Technology. 2018;89:559–565. https://doi.org/10.1016/j.lwt.2017.11.014
7. Kim YHB, Kemp R, Samuelsson LM. Effects of dry-aging on meat quality attributes and metabolite profiles of beef loins. Meat Science. 2016;111:168–176. https://doi.org/10.1016/j.meatsci.2015.09.008
8. Kudryashov LS. Meat: maturation and salting. Kemerovo: Kuzbassvuzizdat; 1992. 206 p. (In Russ.).
9. Domínguez R, Pateiro M, Munekata PES, Zhang W, Garcia-Oliveira P, Carpena M, et al. Protein oxidation in muscle foods: A comprehensive review. Antioxidants. 2022;11(1). https://doi.org/10.3390/antiox11010060
10. Papuc C, Goran GV, Predescu CN, Nicorescu V. Mechanisms of oxidative processes in meat and toxicity induced by postprandial degradation products: A review. Comprehensive Reviews in Food Science and Food Safety. 2017;16(1):96–123. https://doi.org/10.1111/1541-4337.12241
11. Kim YHB, Meyers B, Kim H-W, Liceaga AM, Lemenager RP. Effects of stepwise dry/wet-aging and freezing on meat quality of beef loins. Meat Science. 2017;123:57–63. https://doi.org/10.1016/j.meatsci.2016.09.002
12. da Silva Bernardo AP, da Silva ACM, Francisco VC, Ribeiro FA, Nassu RT, Calkins CR, et al. Effects of freezing and thawing on microbiological and physical-chemical properties of dry-aged beef. Meat Science. 2020;161. https://doi.org/10.1016/j.meatsci.2019.108003
13. Álvarez S, Álvarez C, Hamill R, Mullen AM, O'Neill E. Drying dynamics of meat highlighting areas of relevance to dry-aging of beef. Comprehensive Reviews in Food Science and Food Safety. 2021;20(6):5370–5392. https://doi.org/10.1111/1541-4337.12845
14. Kim J-H, Lee H-J, Shin D-M, Kim T-K, Kim Y-B, Choi Y-S. The dry-aging and heating effects on protein characteristics of beef Longissiumus dorsi. Korean Journal for Food Science of Animal Resources. 2018;38(5):1101–1108. https://doi.org/10.5851/kosfa.2018.e43
15. Zheng J, Han Y, Ge G, Zhao M, Sun W. Partial substitution of NaCl with chloride salt mixtures: Impact on oxidative characteristics of meat myofibrillar protein and their rheological properties. Food Hydrocolloids. 2019;96:36–42. https://doi.org/10.1016/j.foodhyd.2019.05.003
16. Taylor C, Doyle M, Webb D. “The safety of sodium reduction in the food supply: A cross-discipline balancing act” – Workshop proceedings. Critical Reviews in Food Science and Nutrition. 2018;58(10):1650–1659. https://doi.org/10.1080/10408398.2016.1276431
17. Antipova LV, Glotova IA, Rogov IA. Research methods for meat and meat products. Moscow: KolosS; 2001. 376 p. (In Russ.).
18. Li YJ, Li JL, Zhang L, Gao F, Zhou GH. Effects of dietary starch types on growth performance, meat quality and myofibre type of finishing pigs. Meat Science. 2017;131:60–67. https://doi.org/10.1016/j.meatsci.2017.04.237
19. Feng Y-H, Zhang S-S, Sun B-Z, Xie P, Wen K-X, Xu C-C. Changes in physical meat traits, protein solubility, and the microstructure of different beef muscles during post-mortem aging. Foods. 2020;9(6). https://doi.org/10.3390/foods9060806
20. Xia T, Cao Y, Chen X, Zhang Y, Xue X, Han M, et al. Effects of chicken myofibrillar protein concentration on protein oxidation and water holding capacity of its heat-induced gels. Journal of Food Measurement and Characterization. 2018;12(4):2302–2312. https://doi.org/10.1007/s11694-018-9847-8
21. Pérez-Juan M, Flores M, Toldrá F. Effect of ionic strength of different salts on the binding of volatile compounds to porcine soluble protein extracts in model systems. Food Research International. 2007;40(6):687–693. https://doi.org/10.1016/j.foodres.2006.11.013
22. Ma J, Wang X, Li Q, Zhang L, Wang Z, Han L, et al. Oxidation of myofibrillar protein and crosslinking behavior during processing of traditional air-dried yak (Bos grunniens) meat in relation to digestibility. LWT. 2021;142. https://doi.org/10.1016/j.lwt.2021.110984
23. Chelh I, Gatellier, Santé-Lhoutellier V. Technical note: A simplified procedure for myofibril hydrophobicity determination. Meat Science. 2006;74(4):681–683. https://doi.org/10.1016/j.meatsci.2006.05.019
24. Timofeyev MA, Shatilina ZM, Protopopova MV, Bedulina DS, Pavlichenko VV, Kolesnichenko AV, et al. Thermal stress defense in freshwater amphipods from contrasting habitats with emphasis on small heat shock proteins (sHSPs). Journal of Thermal Biology. 2009;34(6):281–285. https://doi.org/10.1016/j.jtherbio.2009.03.008
25. Terevinto A, Cabrera MC, Saadoun A. Influence of feeding system on lipids and proteins oxidation, and antioxidant enzymes activities of meat from Aberdeen Angus steers. Journal of Food and Nutrition Research. 2015;3(9):581–586.
26. Zeng Z, Li C, Ertbjerg P. Relationship between proteolysis and water-holding of myofibrils. Meat Science. 2017;131:48–55. https://doi.org/10.1016/j.meatsci.2017.04.232
27. Santos MD, Delgadillo I, Saraiva JA. Extended preservation of raw beef and pork meat by hyperbaric storage at room temperature. International Journal of Food Science and Technology. 2020;55(3):1171–1179. https://doi.org/10.1111/ijfs.14540
28. Chernukha IM, Kovalev LI, Mashentseva NG, Kovaleva MA, Vostrikova NL. Detection of protein aggregation markers in raw meat and finished products. Foods and Raw Materials. 2019;7(1):118–123. https://doi.org/10.21603/2308-4057-2019-1-118-123
29. Feng Y-H, Zhang S-S, Sun B-Z, Xie P, Wen K-X, Xu C-C. Changes in physical meat traits, protein solubility, and the microstructure of different beef muscles during post-mortem aging. Foods. 2020;9(6). https://doi.org/10.3390/foods9060806
30. Liu J, Arner A, Puolanne E, Ertbjerg P. On the water-holding of myofibrils: Effect of sarcoplasmic protein denaturation. Meat Science. 2016;119:32–40. https://doi.org/10.1016/j.meatsci.2016.04.020
31. Zhang W, Xiao S, Ahn DU. Protein oxidation: Basic principles and implications for meat quality. Critical Reviews in Food Science and Nutrition. 2013;53(11):1191–1201. https://doi.org/10.1080/10408398.2011.577540
32. Zecca E. Investigating the role of surface hydrophobicity in protein aggregation. PhD diss. Storrs: University of Connecticut; 2017. 1488 p.
33. Hellwig M. The chemistry of protein oxidation in food. Angewandte Chemie – International Edition. 2019;58(47):16742–16763. https://doi.org/10.1002/anie.201814144
34. Pateiro M, Munekata PE, Cittadini A, Domínguez R, Lorenzo JM. Metallic-based salt substitutes to reduce sodium content in meat products. Current Opinion in Food Science. 2021;38:21–31. https://doi.org/10.1016/j.cofs.2020.10.029
35. Cittadini A, Domínguez R, Gómez B, Pateiro M, Pérez-Santaescolástica C, López-Fernández O, et al. Effect of NaCl replacement by other chloride salts on physicochemical parameters, proteolysis and lipolysis of dry-cured foal “cecina”. Journal of Food Science and Technology. 2020;57:1628–1635. https://doi.org/10.1007/s13197-019-04195-6
36. Han Z, Cai M-J, Cheng J-H, Sun D-W. Effects of microwave and water bath heating on the interactions between myofibrillar protein from beef and ketone flavour compounds. International Journal of Food Science and Technology.2019;54(5):1787–1793. https://doi.org/10.1111/ijfs.14079
37. Hellwig M. Analysis of protein oxidation in food and feed products. Journal of Agricultural and Food Chemistry. 2020;68(46):12870–12885. https://doi.org/10.1021/acs.jafc.0c00711
38. Zhang YM, Ertbjerg P. Effects of frozen-then-chilled storage on proteolytic enzyme activity and water-holding capacity of pork loin. Meat Science. 2018;145:375–382. https://doi.org/10.1016/j.meatsci.2018.07.017
39. Guan F, Chen Y, Zhao S, Chen Z, Yu C, Yuan Y. Effect of slurry ice during storage on myofibrillar protein of Pseudosciaena crocea. Food Science and Nutrition. 2021;9(7):3806–3814. https://doi.org/10.1002/fsn3.2355
40. Gurinovich GV, Patrakova IS, Seregin SA, Gargaeva AG, Alekseevnina OYa, Myshalova OM, et al. Biological value of semi-smoked sausages with cedar oil cake. Foods and Raw Materials. 2020;8(1):30–39. https://doi.org/10.21603/2308-4057-2020-1-30-39