Investigation of muscle-specific beef color stability at different ultimate pHs
2
조회
0
다운로드
1
인용
0
참고문헌
키워드
초록
Objective: This study was aimed to investigate the muscle-specific beef color stability at normal and high ultimate pHs. Methods: The impact of muscle (Longissimus lumborum [LL] vs psoas major [PM]) and pH (normal ultimate pH [Np] vs high pH dark cutting beef [Hp]) on color stability, indicated by basic color traits, metmyoglobin reducing activity (MRA) and oxygen consumption (OC), as well as the lipid oxidation, were determined over 7 days of display at 4°C. Results: Hp-LL had the highest pH (6.92), followed by Hp-PM (6.01), Np-PM (5.76), and Np-LL (5.52). Hp-LL had increased (p<0.05) a*, chroma and % oxymyoglobin during display. Hp-LL also had the highest metmyoglobin (MMb) reducing activity and OC among all the samples, thus, the greatest color stability, although very dark throughout storage, with lowest values for lightness (L*) and yellowness (b*). Np-LL also exhibited relatively high color stability, as a result of its lower % MMb and OC and higher MRA than psoas muscle samples. The 0.2 unit difference of the pH between Hp and Np psoas muscle, resulted in the difference of the color intensity, not the color stability. Interestingly, high pH psoas muscle (Hp-PM) did not have better color stability than Np-PM, and in fact had lower color stability than even Np-LL. The similar level of OC and lipid oxidation cannot explain the difference in color stability between Hp-PM and Np-LL. Conclusion: The Hp does not always show better color stability compared with Np beef, which depends on the muscle type. The balance of MRA and OC is important to keep the color in great intensity and stability in the meantime.
Abstract
Objective: This study was aimed to investigate the muscle-specific beef color stability at normal and high ultimate pHs. Methods: The impact of muscle (Longissimus lumborum [LL] vs psoas major [PM]) and pH (normal ultimate pH [Np] vs high pH dark cutting beef [Hp]) on color stability, indicated by basic color traits, metmyoglobin reducing activity (MRA) and oxygen consumption (OC), as well as the lipid oxidation, were determined over 7 days of display at 4°C. Results: Hp-LL had the highest pH (6.92), followed by Hp-PM (6.01), Np-PM (5.76), and Np-LL (5.52). Hp-LL had increased (p<0.05) a*, chroma and % oxymyoglobin during display. Hp-LL also had the highest metmyoglobin (MMb) reducing activity and OC among all the samples, thus, the greatest color stability, although very dark throughout storage, with lowest values for lightness (L*) and yellowness (b*). Np-LL also exhibited relatively high color stability, as a result of its lower % MMb and OC and higher MRA than psoas muscle samples. The 0.2 unit difference of the pH between Hp and Np psoas muscle, resulted in the difference of the color intensity, not the color stability. Interestingly, high pH psoas muscle (Hp-PM) did not have better color stability than Np-PM, and in fact had lower color stability than even Np-LL. The similar level of OC and lipid oxidation cannot explain the difference in color stability between Hp-PM and Np-LL. Conclusion: The Hp does not always show better color stability compared with Np beef, which depends on the muscle type. The balance of MRA and OC is important to keep the color in great intensity and stability in the meantime.
참고문헌 (39)
- Mancini RA, "Current research in meat color", Meat Sci, 71, pp.100~121 (2005)[DOI]
- Suman SP, "Myoglobin chemistry and meat color", Annu Rev Food Sci Technol, 4, pp.79~99 (2013)[DOI]
- Smith GC, "Antioxidants in muscle foods: nutritional strategies to improve quality", pp.397~426 (2000), Wiley Interscience
- McKenna DR, "National Beef Quality Audit-2000: survey of targeted cattle and carcass characteristics related to quality, quantity, and value of fed steers and heifers", J Anim Sci, 80, pp.1212~1222 (2002)[DOI]
- McKenna DR, "Biochemical and physical factors affecting discoloration characteristics of 19 bovine muscles", Meat Sci, 70, pp.665~682 (2005)[DOI]
- Seyfert M, "Color stability, reducing activity, and cytochrome c oxidase activity of five bovine muscles", J Agric Food Chem, 54, pp.8919~8925 (2006)[DOI]
- Joseph P, "Proteomics of muscle-specific beef color stability", J Agric Food Chem, 60, pp.3196~3203 (2012)[DOI]
- Canto ACVCS, "Color attributes and oxidative stability of longissimus lumborum and psoas major muscles from Nellore bulls", Meat Sci, 121, pp.19~26 (2016)[DOI]
- Ashmore CR, "Respiration of mitochondria isolated from dark-cutting beef", J Anim Sci, 33, pp.574~577 (1971)[DOI]
- Ponnampalam EN, "Causes and contributing factors to"dark cutting"meat : current trends and future directions : a review", Compr Rev Food Sci Food Saf, 16, pp.400~430 (2017)[DOI]
- Hughes J, "High pH in beef longissimus thoracis reduces muscle fibre transverse shrinkage and light scattering which contributes to the dark colour", Food Res Int, 101, pp.228~238 (2017)[DOI]
- English AR, "Effects of aging on the fundamental color chemistry of dark-cutting beef", J Anim Sci, 94, pp.4040~4048 (2016)[DOI]
- McKeith RO, "Mitochondrial abundance and efficiency contribute to lean color of dark cutting beef", Meat Sci, 116, pp.165~173 (2016)[DOI]
- Wulf DM, "Relationships among glycolytic potential, dark cutting(dark, firm, and dry)beef, and cooked beef palatability", J Anim Sci, 80, pp.1895~1903 (2002)[DOI]
- Holman BWB, "Contrasting the quality traits of aged bolar blade, topside and striploin cuts sourced from dark cutting and control Australian beef carcasses", Meat Sci, 149, pp.24~30 (2019)[DOI]
- Du Y, "Effect of pre-slaughter conditions on beef quality", Scientia Agricultura Sinica, 42, pp.3625~3632 (2009)[DOI]
- AMSA, "Meat color measurement guidelines" (2012), American Meat Science Association
- Mancini RA, "Effects of data expression, sample location, and oxygen partial pressure on initial nitric oxide metmyoglobin formation and metmyoglobin-reducing-activity measurement in beef muscle", Meat Sci, 79, pp.244~251 (2008)[DOI]
- Sammel LM, "Comparison of assays for metmyoglobin reducing ability in beef inside and outside semimembranosus muscle", J Food Sci, 67, pp.978~984 (2002)[DOI]
- Madhavi DL, "Aging and processing affect color, metmyoglobin reductase and oxygen consumption of beef muscles", J Food Sci, 58, pp.939~942 (1993)[DOI]
- Siu GM, "A survey of the malonaldehyde content of retail meats and fish", J Food Sci, 43, pp.1147~1149 (1978)[DOI]
- Yu Q, "Comparative proteomics to reveal muscle-specific beef color stability of Holstein cattle during post-mortem storage", Food Chem, 229, pp.769~778 (2017)[DOI]
- Lefaucheur L, "A second look into fibre typing--relation to meat quality", Meat Sci, 84, pp.257~270 (2010)[DOI]
- England EM, "Excess glycogen does not resolve high ultimate pH of oxidative muscle", Meat Sci, 114, pp.95~102 (2016)[DOI]
- Gardner GE, "Sheep genotype, age and muscle type affect the expression of metabolic enzyme markers", Aust J Exp Agric, 47, pp.1180~1189 (2007)[DOI]
- Rule DC, "Applied muscle biology and meat science", pp.47~74 (2009), Taylor & Francis Group
- Sawyer JT, "Fresh and cooked color of dark-cutting beef can be altered by post-rigor enhancement with lactic acid", Meat Sci, 83, pp.263~270 (2009)[DOI]
- Ma D, "Metabolomics profiling to determine the effect of postmortem aging on color and lipid oxidative stabilities of different bovine muscles", J Agric Food Chem, 65, pp.6708~6716 (2017)[DOI]
- Mahmood S, "Proteomics of dark cutting longissimus thoracis muscle from heifer and steer carcasses", Meat Sci, 137, pp.47~57 (2018)[DOI]
- Mancini RA, "Muscle-specific mitochondrial functionality and its influence on fresh beef color stability", J Food Sci, 83, pp.2077~2082 (2018)[DOI]
- Abril M, "Beef colour evolution as a function of ultimate pH", Meat Sci, 58, pp.69~78 (2001)[DOI]
- Apple JK, "Lactic acid enhancement can improve the fresh and cooked color of dark-cutting beef", J Anim Sci, 89, pp.4207~4220 (2011)[DOI]
- Holman BWB, "Using instrumental(CIE and reflectance)measures to predict consumers' acceptance of beef colour", Meat Sci, 127, pp.57~62 (2017)[DOI]
- Wu W, "Towards muscle-specific meat color stability of Chinese Luxi yellow cattle : A proteomic insight into post-mortem storage", J Proteomics, 147, pp.108~118 (2016)[DOI]
- Kim YH, "Role of lactate dehydrogenase in metmyoglobin reduction and color stability of different bovine muscles", Meat Sci, 83, pp.376~382 (2009)[DOI]
- Ke Y, "Effects of muscle-specific oxidative stress on cytochrome c release and oxidation-reduction potential properties", J Agric Food Chem, 65, pp.7749~7755 (2017)[DOI]
- Tang J, "Mitochondrial reduction of metmyoglobin : ? dependence on the electron transport chain", J Agric Food Chem, 53, pp.5449~5455 (2005)[DOI]
- Purohit A, "Effects of heme and nonheme iron on meat quality characteristics during retail display and storage", J Food Meas Charact, 9, pp.175~185 (2015)[DOI]
- Jeong JY, "Discoloration characteristics of 3 major muscles from cattle during cold storage", J Food Sci, 74, pp.C1~C5 (2009)[DOI]
