Skip to main content
SpringerLink
Log in

Effects of Different Packaging Systems on Beef Tenderness Through Protein Modifications

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

Abstract

The main purpose of this study was to investigate effects of three packaging methods on beef tenderness via protein oxidative modifications. Tenderness, protein oxidation, μ-calpain activation, and protein proteolysis of bovine longissimus dorsi (LD) muscle were measured during 10 days (d) of chilled storage. Compared with beef samples from vacuum packaging (VP), beef samples from air packaging (AP) and modified atmosphere packaging (MAP) showed significantly lower free thiol group and higher carbonyl group content, while tenderness was lower after 7 and 10 d of chilled storage, respectively (p < 0.05). μ-Calpain activity was less in beef samples from AP and MAP compared with VP at d 4 and 7 of postmortem storage (p < 0.05). Desmin showed decreased proteolysis in beef samples from AP and MAP compared with VP after 4 and 7 d of storage (p < 0.05). The results above indicated that the reduction in tenderness of beef samples from AP and MAP compared to VP was closely associated with protein modifications including oxidation, proteolysis, and enzyme activation of bovine LD muscle during postmortem storage.

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

Access this article

Log in via an institution

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

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6

Similar content being viewed by others

Abbreviations

LD:

Longissimus dorsi

VP:

Vacuum packaging

AP:

Air packaging

MAP:

Modified atmosphere packaging

MCE:

β-Mercaptoethanol

TCA:

Trichloroacetic acid

DNPH:

2,4-Dinitrophenylhydrazine

DTNB:

5,5′-Dithiobis-2-nitrobenzoate

BB:

Bromophenol blue

SDS-PAGE:

Sodium dodecyl sulfate polyacrylamide gel electrophoresis

d:

Day or days

References

  • Amici, A., Levine, R. L., Tsai, L., & Stadtman, E. R. (1989). Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed reactions. The Journal of Biological Chemistry, 264(6), 3341–3346.

    CAS  Google Scholar 

  • Arvanitoyannis, I. S., & Stratakos, A. C. (2012). Application of modified atmosphere packaging and active/smart technologies to red meat and poultry: a review. Food and Bioprocess Technology, 5, 1423–1446.

    Article  CAS  Google Scholar 

  • Balogh, J., Li, Z., Paulin, D., & Arner, A. (2005). Desmin filaments influence myofilament spacing and lateral compliance of slow skeletal, muscle fibers. Biophisical Journal, 88(2), 1156–1165.

    Article  CAS  Google Scholar 

  • Clausen, I., Jakobsen, M., Ertbjerg, P., & Madsen, N. T. (2009). Modified atmosphere packaging affects lipid oxidation, myofibrillar fragmentation index and eating quality of beef. Packaging Technology and Science, 22, 85–96.

    Article  CAS  Google Scholar 

  • Davies, M. J., & Dean, R. T. (2003). Radical-mediated protein oxidation. (Eds.) Oxford Science Publications, Oxford.

  • Davis, K. J., Sebranek, J. G., Huff-Lonergan, E., & Lonergan, S. M. (2004). The effects of aging on moisture-enhanced pork loins. Meat Science, 66(3), 519–524.

    Article  CAS  Google Scholar 

  • Ducastaing, A., Valin, C., Schollmeyer, J., & Cross, R. (1985). Effects of electrical stimulation on postmortem changes in the activities of two Ca2+ dependent neutral proteinases and their inhibitor in beef muscle. Meat Science, 15(4), 193–202.

    Article  CAS  Google Scholar 

  • Gornall, A. G., Bardawill, C. J., & David, M. M. (1949). Determination of serum proteins by means of the biuret reaction. Journal of Biological Chemistry, 177(2), 751–766.

    CAS  Google Scholar 

  • Hofmann, K., & Reiner, H. (1978). Sulfhydryl and disulfide groups in meats. Advances in Food Research, 24(2), 1–111.

    Article  CAS  Google Scholar 

  • Huff-Lonergan, E., & Lonergan, S. M. (2005). Mechanism of water-holding capacity of meat: the role of postmortem biochemical and structural changes. Meat Science, 71(1), 194–204.

    Article  CAS  Google Scholar 

  • Huff-Lonergan, E., Mitsuhashi, T., Beekman, D. D., Parrish, J. F. C., Olson, D. G., & Robson, R. M. (1996). Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. Journal of Animal Science, 74, 993–1008.

    CAS  Google Scholar 

  • Huff-Lonergan, E., Zhang, W. G., & Lonergan, S. M. (2010). Biochemistry of postmortem muscle—lessons on mechanisms of meat tenderization. Meat Science, 86(1), 184–195.

    Article  CAS  Google Scholar 

  • Hynes, R. O. (1992). Integrins: versatility, modulation, and signalling in cell adhesion. Cell, 69(1), 11–25.

    Article  CAS  Google Scholar 

  • Jeremiah, L. E. (2001). Packaging alternatives to deliver fresh meats using short- or long-term distribution. Food Research International, 34, 749–772.

    Article  Google Scholar 

  • José, M. L., & María, G. (2012). Shelf life of fresh foal meat under MAP, overwrap and vacuum packaging conditions. Meat Science, 92, 610–618.

    Article  Google Scholar 

  • Kanner, J. (1994). Oxidative processes in meat and meat products: quality implications. Meat Science, 36, 169–189.

    Article  CAS  Google Scholar 

  • Koohmaraie, M. (1996). Biochemical factors regulating the toughening and tenderization processes of meat. Meat Science, 43(Supplement 1), 193–201.

    Article  Google Scholar 

  • Koohmaraie, M., Seideman, S. C., Schollmeyer, J. E., Dutson, T. R., & Crouse, J. D. (1987). Effect of postmortem storage on Ca2+-dependent proteases, their inhibitor and myofibril fragmentation. Meat Science, 19, 187–196.

    Article  CAS  Google Scholar 

  • Lagerstedt, Å., Lundström, K., & Lindahl, G. (2011). Influence of vacuum or high-oxygen modified atmosphere packaging on quality of beef M. longissimus dorsi steaks after different ageing times. Meat Science, 87(2), 101–106.

    Article  CAS  Google Scholar 

  • Lametsch, R., Lonergan, S., & Huff-Lonergan, E. (2008). Disulfide bond with mμ-calpain active site inhibits activity and autolysis. Biochimica et Biophysica Acta, 1784(9), 1215–1221.

    Article  CAS  Google Scholar 

  • Li, C. B., Zhou, G. H., & Xu, X. L. (2010). Dynamic changes of beef intramuscular connective tissue and muscle fiber during heating and their effects on beef shear force. Food and Bioprocess Technology, 3, 521–527.

    Article  Google Scholar 

  • Li, X., Lindahl, G., Zamaratskaia, G., & Lundström, K. (2012). Influence of vacuum skin packaging on color stability of beef longissimus lumborum compared with vacuum and high-oxygen modified atmosphere packaging. Meat Science, 92, 604–609.

    Article  CAS  Google Scholar 

  • Lindahl, G., Lagerstedt, Å., Ertbjerg, P., Sampels, S., & Lundström, K. (2010). Ageing of large cuts of beef loin in vacuum or high oxygen modified atmosphere—effect on shear force, calpain activity, desmin degradation and protein oxidation. Meat Science, 85, 160–166.

    Article  CAS  Google Scholar 

  • Lund, M. N., Lametsh, R., Hviid, M. S., Jensen, O. L., & Skibsted, L. H. (2007). High oxygen packaging atmosphere influences protein oxidation and tenderness of porcine longissimus dorsi during chill storage. Meat Science, 77(3), 295–303.

    Article  CAS  Google Scholar 

  • Lund, M. N., Heinonen, M., Boron, C. P., & Este´vez, M. (2011). Protein oxidation in muscle foods: a review. Molecular Nutrition and Food Research, 55(1), 83–95.

    Article  CAS  Google Scholar 

  • McMillin, K. W. (2008). Where is MAP going? A review and future potential of modified atmosphere packaging for meat. Meat Science, 80, 43–65.

    Article  CAS  Google Scholar 

  • Melody, J. L., Lonergan, S. M., Rowe, L. J., Huiatt, T. W., Mayes, M. S., & Huff-Lonergan, E. (2004). Early postmortem biochemical factors influence tenderness and water holding capacity of three porcine muscles. Journal of Animal Science, 82(4), 1195–1205.

    CAS  Google Scholar 

  • Neumann, N. P. (1972). Oxidation with hydrogen peroxide. Methods in Enzymology, 25, 393–400.

    Article  CAS  Google Scholar 

  • Paredi, G., Raboni, S., Bendixen, E., Almeida, A., & Andrea, M. (2012). “Muscle to meat” molecular events and technological transformations: the proteomics insight. Journal of Proteomics, 75(14), 4275–4289.

    Article  CAS  Google Scholar 

  • Park, D., Xiong, Y. L., & Alderton, A. L. (2006). Concentration effects of hydroxyl radical oxidizing systems on biochemical properties of porcine muscle myofibrillar protein. Food Chemistry, 101(3), 1239–1246.

    Article  Google Scholar 

  • Penny, I. F., & Dransfield, E. (1979). The relationship between toughness and troponin-T in conditioned beef. Meat Science, 3(4), 135–138.

    Article  CAS  Google Scholar 

  • Pulford, D. J., Dobbie, P., Fraga Vazquez, S., Fraser-Smith, E., Frost, D. A., & Morris, C. A. (2009). Variation in bull beef quality due to ultimate muscle pH is correlated to endopeptidase and small heat shock protein levels. Meat Science, 83(1), 1–9.

    Article  CAS  Google Scholar 

  • Rowe, L. J., Maddock, K. R., Lonergan, S. M., & Huff-Lonergan, E. (2004). Oxidative environments decrease tenderization of beef steaks through inactivation of m-calpain. Journal of Animal Science, 82(11), 3254–3266.

    CAS  Google Scholar 

  • Santos, E. M., Jaime, I., Rovira, J., Lyhs, U., KoRkeala, U., & Bjorkroth, J. (2005). Characterization and identification of lactic acid bacteria in “morcila de burgos”. International Journal of Microbiology, 97, 285–296.

    Article  CAS  Google Scholar 

  • Sanz, A., Ripoll, G., Blasco, I., Alvarez-Rodríguez, J., & Albertí, P. (2011). Performance of yearling, bull and steer of serrana de teruel breed. In A. Sanz, I. Casasús, M. Joy, J. Álvarez-Rodriguez, J. H. Calvo, B. Panea, P. Muñoz, & J. Balcells (Eds.), XIV Jornadas sobre Producción Animal (Vol. II, pp. 745–747). Zaragoza: AIDA.

    Google Scholar 

  • Sentandreu, M. A., Coulis, G., & Ouali, A. (2002). Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends in Food Science and Technology, 13(12), 400–421.

    Article  CAS  Google Scholar 

  • Shackelford, S. D., Wheeler, T. L., Meade, M. K., Reagan, J. O., Byrnes, B. L., & Koohmaraie, M. (2001). Consumer impressions of tender select beef. Journal of Animal Science, 79(10), 2605–2614.

    CAS  Google Scholar 

  • Taylor, R. G., Geesink, G. H., Thompson, V. F., Koohmaraie, M., & Goll, D. E. (1995). Is Z-disk degradation responsible for postmortem tenderization? Journal of Animal Science, 73(5), 1351–1367.

    CAS  Google Scholar 

  • Veiseth, E., Shackelford, S. D., Wheeler, T. L., & Koohmaraie, M. (2001). Effect of postmortem storage on μ-calpain and m-calpain in ovine skeletal muscle. Journal of Animal Science, 79(6), 1502–1508.

    CAS  Google Scholar 

  • Xiao, S., Zhang, W. G., Lee, E. J., Ma, C. W., & Ahn, D. U. (2011). Effects of diet, packaging, and irradiation on protein oxidation, lipid oxidation, and color of raw broiler thigh meat during refrigerated storage. Poultry Science, 90(6), 1348–1357.

    Article  CAS  Google Scholar 

  • Xiong, Y. L. (2000). Protein oxidation and implications for muscle food quality. In E. A. Decker, C. L. Faustman, & C. J. Lopez-Bote (Eds.), Antioxidants in muscle foods (pp. 85–111). New York: John Wiley & Sons, Inc.

    Google Scholar 

  • Xiong, Y. L., Park, D., & Ooizumi, T. (2009). Variation in the cross-linking pattern of porcine myofibrillar protein exposed to three oxidative environments. Journal of Agricultural and Food Chemistry, 57(1), 153–159.

    Article  CAS  Google Scholar 

  • Yongsawatdigul, J., & Park, J. W. (2003). Thermal denaturation and aggregation of threadfin bream actomyosin. Food Chemistry, 83(3), 409–416.

    Article  CAS  Google Scholar 

  • Zakrys-Waliwander, P. I., O’Sullivan, M. G., O’Neill, E. E., & Kerry, J. P. (2012). The effects of high oxygen modified atmosphere packaging on protein oxidation of bovine M. longissimus dorsi muscle during chilled storage. Food Chemistry, 131, 527–532.

    Article  CAS  Google Scholar 

  • Zhang, W. G., Lonergan, S. M., Gardner, M. A., & Huff-Lonergan, E. (2006). Contribution of postmortem changes of integrin, desmin and μ-calpain to variation in water holding capacity of pork. Meat Science, 74(3), 578–585.

    Article  CAS  Google Scholar 

  • Zhang, W. G., Xiao, S., Lee, E. J., & Ahn, D. U. (2011). Consumption of oxidized oil increases oxidative stress in broilers and affects the quality of breast meat. Journal of Agricultural and Food Chemistry, 59(3), 969–974.

    Article  CAS  Google Scholar 

  • Zhang, W. G., Xiao, S., & Ahn, D. U. (2013). Protein oxidation: basic principles and implications for meat quality. Critical Reviews in Food Science and Nutrition, 53(11), 1191–1201.

    Article  CAS  Google Scholar 

Download references

Acknowledgments

The authors would like to thank the general manager and technical workers in Yurun Food Co. Ltd. (Fuyang, Anhui, China) for their cooperation and their assistance in the collection and packaging of beef samples. This study was supported by the National Natural Science Foundation of China (31271899) and the Ministry of Science and Technology of China (2012BAD28B03).

Author information

Authors and Affiliations

  1. Key Laboratory of Meat Processing and Quality Control, Ministry of Education China, Synergetic Innovation Center of Food Safety and Nutrition, Jiangsu Innovation Center of Meat Production and Processing, College of Food Science and Technology, Nanjing Agricultural University, Nanjing, 210095, China

    Qing-quan Fu, Rui Liu, Wan-gang Zhang, Yu-pin Li, Juan Wang & Guang-hong Zhou

  2. School of Biochemical and Environmental Engineering, Nanjing Xiaozhuang University, Nanjing, 211171, China

    Qing-quan Fu

Authors
  1. Qing-quan Fu
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Rui Liu
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Wan-gang Zhang
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Yu-pin Li
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Juan Wang
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Guang-hong Zhou
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Wan-gang Zhang.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Fu, Qq., Liu, R., Zhang, Wg. et al. Effects of Different Packaging Systems on Beef Tenderness Through Protein Modifications. Food Bioprocess Technol 8, 580–588 (2015). https://doi.org/10.1007/s11947-014-1426-3

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11947-014-1426-3

Keywords

Search

Navigation