The quality differences and Raman spectroscopic features of beef, which was frozen for 0–11 months followed by being thawed and displayed for 0–21 days were investigated. Frozen storage did not significantly affect the color blooming ability, in which minimal change in the color parameter redness and yellowness values of thawed beef in the later stage of frozen storage occurred. As such, it was not able to distinguish between frozen-thawed and non-frozen-thawed meat directly in terms of color changes. The total viable count and the total volatile basic nitrogen content increased sharply in the frozen-thawed meat subjected to 11-month frozen storage. The thiobarbituric acid reactive substances value increased dramatically from 0.18 to 0.29 mg/kg during 11-month frozen storage. Raman spectroscopy data showed that the stability of the protein secondary structure of thawed beef became worse after 3 months of frozen storage, of which the relative content of α-helix and β-sheet decreased significantly to 21.46% and 28.94% during 11-month frozen storage, respectively. The findings suggest that quality deterioration occurred for the frozen-thawed beef, and Raman spectroscopy could be a potential method to distinguish unfrozen meat from frozen-thawed meat.
X. Chen, Y. Zhang, X. Yang, et al., Shelf-life and microbial community dynamics of super-chilled beef imported from Australia to China, Food Res. Int. 120 (2019) 784–792. https://doi.org/10.1016/j.foodres.2018.11.039.
H. Kiani, D. W. Sun, Water crystallization and its importance to freezing of foods: a review, Trends Food Sci. Technol. 22(8) (2011) 407–426. https://doi.org/10.1016/j.jpgs.2011.04.011.
Q. Jiang, N. Nakazawa, Y. Hu, et al., Changes in quality properties and tissue histology of lightly salted tuna meat subjected to multiple freeze-thaw cycles, Food Chem. 293 (2019) 178–186. https://doi.org/10.1016/j.foodchem.2019.04.091.
C. E. Coombs, B. W. Holman, M. A. Friend, et al., Long-term red meat preservation using chilled and frozen storage combinations: a review, Meat Sci. 125 (2017) 84–94. https://doi.org/10.1016/j.meatsci.2016.11.025.
M. Zhang, F. Li, X. Diao, et al., Moisture migration, microstructure damage and protein structure changes in porcine longissimus muscle as influenced by multiple freeze-thaw cycles, Meat Sci. 133 (2017) 10–18. https://doi.org/10.1016/j.meatsci.2017.05.019.
Y. Zhang, E. Puolanne, P. Ertbjerg, Mimicking myofibrillar protein denaturation in frozen-thawed meat: effect of pH at high ionic strength, Food Chem. 338 (2021) 128017. https://doi.org/10.1016/j.foodchem.2020.128017.
Y. Zhang, P. Ertbjerg, On the origin of thaw loss: relationship between freezing rate and protein denaturation, Food Chem. 299 (2019) 125104. https://doi.org/10.1016/j.foodchem.2019.125104.
Å. Lagerstedt, L. Enfält, L. Johansson, et al., Effect of freezing on sensory quality, shear force and water loss in beef M. longissimus dorsi, Meat Sci. 80(2) (2008) 457–461. https://doi.org/10.1016/j.meatsci.2008.01.009.
C. Leygonie, T. J. Britz, L. C. Hoffman, Impact of freezing and thawing on the quality of meat, Meat Sci. 91(2) (2012) 93–98. https://doi.org/10.1016/j.meatsci.2012.01.013.
E. Muela, P. Monge, C. Sañudo, et al., Sensory quality of lamb following long-term frozen storage, Meat Sci. 114 (2016) 32–37. https://doi.org/10.1016/j.meatsci.2015.12.001.
H. M. Velioğlu, H. T. Temiz, I. H. Boyaci, Differentiation of fresh and frozen-thawed fish samples using Raman spectroscopy coupled with chemometric analysis, Food Chem. 172 (2015) 283–290. https://doi.org/10.1016/j.foodchem.2014.09.073.
A. M. Herrero, Raman spectroscopy a promising technique for quality assessment of meat and fish: a review, Food Chem. 107(4) (2008) 1642–1651. https://doi.org/10.1016/j.foodchem.2007.10.014.
A. M. Herrero, P. Carmona, M. Careche, Raman spectroscopic study of structural changes in hake ( Merluccius merluccius L.) muscle proteins during frozen storage, J. Agric. Food Chem. 52(8) (2004) 2147–2153. https://doi.org/10.1021/jf034301e.
G. Siu, H. Draper, A survey of the malonaldehyde content of retail meats and fish, J. Food Sci. 43(4) (1978) 1147–1149. https://doi.org/10.1111/j.1365-2621.1978.tb15256.x.
X. Yang, Y. Zhang, L. Zhu, et al., Effect of packaging atmospheres on storage quality characteristics of heavily marbled beef longissimus steaks, Meat Sci. 117 (2016) 50–56. https://doi.org/10.1016/j.meatsci.2016.02.030.
C. Wang, H. Wang, X. Li, et al., Effects of oxygen concentration in modified atmosphere packaging on water holding capacity of pork steaks, Meat Sci. 148 (2019) 189–197. https://doi.org/10.1016/j.meatsci.2018.10.001.
S. Cheng, X. Wang, R. Li, et al., Influence of multiple freeze-thaw cycles on quality characteristics of beef semimembranous muscle: with emphasis on water status and distribution by LF-NMR and MRI, Meat Sci. 147 (2019) 44–52. https://doi.org/10.1016/j.meatsci.2018.08.020.
H. Yang, D. L. Hopkins, Y. Zhang, et al., Preliminary investigation of the use of Raman spectroscopy to predict beef spoilage in different types of packaging, Meat Sci. 165 (2020) 108136. https://doi.org/10.1016/j.meatsci.2020.108136.
E. Muela, C. Sañudo, M. Campo, et al., Effect of freezing method and frozen storage duration on instrumental quality of lamb throughout display, Meat Sci. 84(4) (2010) 662–669. https://doi.org/10.1016/j.meatsci.2009.10.028.
X. Lu, Y. Zhang, L. Zhu, et al., Effect of superchilled storage on shelf life and quality characteristics of M. longissimus lumborum from Chinese Yellow cattle, Meat Sci. 149 (2019) 79–84. https://doi.org/10.1016/j.meatsci.2018.11.014.
B. W. B. Holman, C. E. O. Coombs, S. Morris, et al., Effect of long term chilled (up to 5 weeks) then frozen (up to 12 months) storage at two different sub-zero holding temperatures on beef: 1. Meat quality and microbial loads, Meat Sci. 133 (2017) 133–142. https://doi.org/10.1016/j.meatsci.2017.06.015.
E. Muela, P. Monge, C. Sañudo, et al., Meat quality of lamb frozen stored up to 21 months: instrumental analyses on thawed meat during display, Meat Sci. 102 (2015) 35–40. https://doi.org/10.1016/j.meatsci.2014.12.003.
X. Xia, B. Kong, Q. Liu, et al., Physicochemical change and protein oxidation in porcine longissimus dorsi as influenced by different freeze-thaw cycles, Meat Sci. 83(2) (2009) 239–245. https://doi.org/10.1016/j.meatsci.2009.05.003.
A. Soyer, B. Özalp, Ü. Dalmış, et al., Effects of freezing temperature and duration of frozen storage on lipid and protein oxidation in chicken meat, Food Chem. 120(4) (2010) 1025–1030. https://doi.org/10.1016/j.foodchem.2009.11.042.
M. Bellés, V. Alonso, P. Roncalés, et al., The combined effects of superchilling and packaging on the shelf life of lamb, Meat Sci. 133 (2017) 126–132. https://doi.org/10.1016/j.meatsci.2017.06.013.
I. K. Kluth, V. Teuteberg, M. Ploetz, et al., Effects of freezing temperatures and storage times on the quality and safety of raw turkey meat and sausage products, Poult Sci. 100(9) (2021) 101305. https://doi.org/10.1016/j.psj.2021.101305.
S. Qian, X. Li, H. Wang, et al., Effect of sub-freezing storage (−6, −9 and −12 °C) on quality and shelf life of beef, Int. J. Food Sci. Technol. 53(9) (2018) 2129–2140. https://doi.org/10.1111/ijfs.13800.
J. Melody, S. M. Lonergan, L. Rowe, et al., Early postmortem biochemical factors influence tenderness and water-holding capacity of three porcine muscles, J. Anim Sci. 82(4) (2004) 1195–1205. https://doi.org/10.2527/2004.8241195x.
E. Kirtil, S. Cikrikci, M. J. McCarthy, et al., Recent advances in time domain NMR & MRI sensors and their food applications, Curr. Opin. Food Sci. 17 (2017) 9–15. https://doi.org/10.1016/j.cofs.2017.07.005.
J. Sánchez-Valencia, I. Sánchez-Alonso, I. Martinez, et al., Low-field nuclear magnetic resonance of proton (1H LF-NMR) relaxometry for monitoring the time and temperature history of frozen hake ( Merluccius merluccius L.) muscle, Food Bioprocess Technol. 8 (2015) 2137–2145. https://doi.org/10.1007/s11947-015-1569-x.
S. Ali, W. Zhang, N. Rajput, et al., Effect of multiple freeze-thaw cycles on the quality of chicken breast meat, Food Chem. 173 (2015) 808–814. https://doi.org/10.1016/j.foodchem.2014.09.095.
S. Ngarize, H. Herman, A. Adams, et al., Comparison of changes in the secondary structure of unheated, heated, and high-pressure-treated β-lactoglobulin and ovalbumin proteins using Fourier transform Raman spectroscopy and self-deconvolution, J. Agric. Food Chem. 52(21) (2004) 6470–6477. https://doi.org/10.1021/jf030649y.
X. Li, X. Wei, H. Wang, et al., Relationship between protein denaturation and water holding capacity of pork during postmortem ageing, Food Biophys. 13 (2018) 18–24. https://doi.org/10.1007/s11483-017-9507-2.
T. Sano, T. Ohno, H. Otsuka-Fuchino, et al., Carp natural actomyosin: thermal denaturation mechanism, J. Food Sci. 59(5) (1994) 1002–1008. https://doi.org/10.1111/j.1365-2621.1994.tb08177.x.
Z. J. Bao, J. P. Wu, Y. Cheng, et al., Effects of lipid peroxide on the structure and gel properties of ovalbumin, Process Biochem. 57 (2017) 124–130. https://doi.org/10.1016/j.procbio.2017.03.009.