包装方式对牛肉贮藏过程中蛋白质氧化及降解的影响
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摘要
为探明托盘透氧包装(air packaging,AP)和高氧气调包装(modified atmosphere packaging,MAP,80%O2+20%CO2)对宰后牛肉贮藏过程中对牛肉嫩度影响的潜在机制,以真空包装(vacuum packaging,VP)为对照,选取6头西门塔尔纯种母黄牛背最长肌,分别进行托盘透氧包装、真空包装和高氧气调包装,4℃冷库分别贮藏0、4、7、10 d,分别测定蛋白羰基含量及分布、蛋白表面疏水性值、蛋白质溶解度值以及肌间线蛋白和肌联蛋白的降解变化。结果表明:相对于真空包装组,托盘包装组和高氧气调包装组在宰后贮藏过程中肌细胞外围出现羰基氧化荧光信号显著增加,且不断向细胞内部扩散,说明其蛋白质氧化程度不断增加;宰后贮藏10 d后,托盘透氧包装组和高氧气调包装组的蛋白质表面疏水性显著高于真空包装组(P<0.05),而托盘透氧包装组和高氧气调包装组的蛋白溶解性显著低于真空包装组(P<0.05);宰后贮藏7和10 d,托盘透氧包装组和高氧气调包装组的肌间线蛋白和肌联蛋白的降解显著低于真空包装组(P<0.05),说明托盘透氧包装组和高氧气调包装组抑制了肌间线蛋白和肌联蛋白的降解(P<0.05)。托盘透氧包装组和高氧气调包装组能够提高宰后贮藏过程中蛋白质氧化程度,从而抑制其对牛肉骨骼关键蛋白的降解,该研究可为牛肉贮藏提供理论支撑。
Air packaging(AP), vacuum packaging(VP) and modified atmosphere packaging(MAP) have been widely used during chilled storage in retail meat market. However, different packaging has its advantage and disadvantage. AP can get desirable red color in a short time, but protein oxidation and lipid oxidation occur during cold storage. VP keeps a stable purple color and increases the shelf life of fresh meat. However, VP can cause liquid exudation and product deformation of fresh meat. MAP with 80% oxygen can maintain desirable and stable cherry red color of fresh meat and extend the shelf life of fresh beef. Nevertheless, it can possibly cause protein oxidation and lipid oxidation of fresh meat during chilled storage. Protein oxidation is the covalent modification of proteins induced by reactive oxygen species or by-products of oxidative stress. Previous researches have demonstrated that protein oxidation inhibits μ-calpain activity, which may influence the rate and degree of protein degradation of fresh meat. The aim of this study was to examine effects of AP and high-oxygen MAP(80% O2 + 20% CO2) on the tenderness of beef samples during postmortem cold storage using VP as control. Six longissimus dorsi muscles of Simmental purebred yellow cattle were precooled at 4 for ℃ 24 h, which were then randomly assigned to MAP, VP and AP, and stored for 0, 4, 7 and 10 d respectively at 4℃. The carbonyl content and distribution, the values of protein surface hydrophobicity, the solubility values of myofibrillar protein, sarcoplasmic protein and total protein, and the degradation of desmin and titin were determined, respectively. The results showed that AP and MAP presented the stronger fluorescence light signal in a peripheral area, and the fluorescence light signal spread to the internal cellular environment, which showed that the extent of protein oxidation increased. The values of protein surface hydrophobicity of beef samples from AP and MAP were significantly higher than that of the samples from VP(P<0.05), while the protein solubility values of beef samples from AP and MAP were significantly lower than that of the samples from VP 10 d after the storage(P<0.05). The degradation of desmin and titin of beef samples from AP and MAP was significantly lower compared to the VP 7 and 10 d after the storage(P<0.05), which showed protein oxidation further inhibited the degradation of desmin and titin. Increased protein oxidation under AP and MAP inhibits the degradation of the key protein during postmortem cold storage.
Air packaging(AP), vacuum packaging(VP) and modified atmosphere packaging(MAP) have been widely used during chilled storage in retail meat market. However, different packaging has its advantage and disadvantage. AP can get desirable red color in a short time, but protein oxidation and lipid oxidation occur during cold storage. VP keeps a stable purple color and increases the shelf life of fresh meat. However, VP can cause liquid exudation and product deformation of fresh meat. MAP with 80% oxygen can maintain desirable and stable cherry red color of fresh meat and extend the shelf life of fresh beef. Nevertheless, it can possibly cause protein oxidation and lipid oxidation of fresh meat during chilled storage. Protein oxidation is the covalent modification of proteins induced by reactive oxygen species or by-products of oxidative stress. Previous researches have demonstrated that protein oxidation inhibits μ-calpain activity, which may influence the rate and degree of protein degradation of fresh meat. The aim of this study was to examine effects of AP and high-oxygen MAP(80% O2 + 20% CO2) on the tenderness of beef samples during postmortem cold storage using VP as control. Six longissimus dorsi muscles of Simmental purebred yellow cattle were precooled at 4 for ℃ 24 h, which were then randomly assigned to MAP, VP and AP, and stored for 0, 4, 7 and 10 d respectively at 4℃. The carbonyl content and distribution, the values of protein surface hydrophobicity, the solubility values of myofibrillar protein, sarcoplasmic protein and total protein, and the degradation of desmin and titin were determined, respectively. The results showed that AP and MAP presented the stronger fluorescence light signal in a peripheral area, and the fluorescence light signal spread to the internal cellular environment, which showed that the extent of protein oxidation increased. The values of protein surface hydrophobicity of beef samples from AP and MAP were significantly higher than that of the samples from VP(P<0.05), while the protein solubility values of beef samples from AP and MAP were significantly lower than that of the samples from VP 10 d after the storage(P<0.05). The degradation of desmin and titin of beef samples from AP and MAP was significantly lower compared to the VP 7 and 10 d after the storage(P<0.05), which showed protein oxidation further inhibited the degradation of desmin and titin. Increased protein oxidation under AP and MAP inhibits the degradation of the key protein during postmortem cold storage.
引文
[1]刘泽龙.蛋白质氧化对肉及肉制品持水和水合特性的影响机理研究[D].无锡:江南大学,2012.
[2]Kerry J P,O’grady M N,Hogan S A.Past,current and potential utilisation of active and intelligent packaging systems for meat and muscle-based products:A review[J].Meat Science,2006,74:113-130.
[3]Shacter E.Quantification and significance of protein oxidation in biological samples[J].Drug Metabolism Reviews,2000,32:307-326.
[4]Vitale M,Pérez-Juan M,Lloret E,et al.Effect of aging time in vacuum on tenderness,and color and lipid stability of beef from mature cows during display in high oxygen atmosphere package[J].Meat Science,2014,96:270-277.
[5]孔保华,刁新平.冷却肉包装保鲜技术的研究进展[J].肉类研究,2008,2:54-59.
[6]Skandamis P N,Nychas G E.Preservation of fresh meat with active and modified atmosphere packaging conditions[J].International Journal of Food Microbiology,2002,79:35-45.
[7]Liu C L,Zhang Y M,Yang X M,et al.Potential mechanisms of carbon monoxide and high oxygen packaging in maintaining color stability of different bovine muscles[J].Meat Science,2014,97(2):189-196.
[8]Clausen I,Jakobsen M,Ertbjerg P,et al.Modified atmosphere packaging affects lipid oxidation,myofibrillar fragmentation index and eating quality of beef[J].Packaging Technology and Science,2009,22(2):85-96.
[9]Delles R M,Xiong Y L.The effect of protein oxidation on hydration and water-binding in pork packaged in an oxygen-enriched atmosphere[J].Meat Science,2014,97(2):181-188.
[10]Livingston M,Brewer S,Killifer J,et al.Shelf life characteristics of enhanced modified atmosphere packaged pork[J].Meat Science,2004,68(1):115-122.
[11]Huff-Lonergan E,Lonergan S M.Mechanism of water-holding capacity of meat:The role of postmortem biochemical and structural changes.Meat Science,2005,71(1):194-204.
[12]Lund M N,Heínonen M,Baron C P,et al.Protein oxidation in muscle foods:a review[J].Molecular Nutrition and Food Research,2011,55(1):83-95.
[13]Park D,Xiong Y L,Alderton A L.Concentration effects of hydroxyl radical oxidizing systems on biochemical properties of porcine muscle myofibrillar protein[J].Food Chemistry,2006,101(3):1239-1246.
[14]Gornall A G,Bardawill C J,David M M.Determination of serum proteins by means of the biuret reaction[J].Journal of Biological Chemistry,1949,177(2):751-766.
[15]Astruc T,Marinova P,Labas R,et al.Detection and localization of oxidized proteins in muscle cells by fluorescence microscopy[J].Journal of Agricultural and Food Chemistry,2007,55(23):9554-9558.
[16]Chelh I,Gatellier P,SantéLhoutellier V.Technical note:A simplified procedure for myofibril hydrophobicity determination[J].Meat Science,2006,74(4):681-684.
[17]Joo S T,Kauffman R G,Kim B C,et al.The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water-holding capacity in porcine longissimus muscle[J].Meat Science,1999,52(3):291-297.
[18]Fu Q Q,Liu R,Zhang W G,et al.Effects of different packaging systems on beef tenderness through protein modifications[J].Food and Bioprocess Technology,2015,8(3):580-588.
[19]Li Y P,Liu R,Zhang W G,et al.Effect of nitric oxide onμ?calpain activation,protein proteolysis,and protein oxidation of pork during post-mortem aging[J].Journal of Agriculture and Food Chemistry,2014,62(25):5972-5977.
[20]Stadman E R,Levine R L.Protein oxidation[J].Annals the New York Academy of Sciences,2000,899(1):191-208.
[21]Sheikh M I,Gerdes U.Interaction of phenolsulphonphtalein dyes with rabbit plasma and rabbit serum albumin[J].Archives Internationales de Physiologie et de Biochimie,1978,86:613-623.
[22]Huang Y R,Hua Y F,Qiu A Y.Soybean protein aggregation induced by lipoxygenase catalyzed linoleic acid oxidation[J].Food Research International,2006,39:240-249.
[23]Santé-Lhoutellier V,Aubry L,Gatellier P.Effect of oxidation on in vitro digestibility of skeletal muscle myofibrillar proteins[J].Journal of Agricultural and Food Chemistry,2007,55:5343-5348.
[24]Yarnpakdee S,Benjakul S,Visessanguan W,et al.Thermal properties and heat-induced aggregation of natural actomyosin extracted from goatfish(Mulloidichthys martinicus)muscle as influenced by iced storage[J].Food Hydrocolloids,2009,23:1779-1784.
[25]胡忠良.鸡胸肉肌原纤维蛋白氧化对其热诱导凝胶和理化特性的影响[D].南京:南京农业大学,2012.
[26]Xue M,Huang F,Huang M,et al.Influence of oxidation on myofibrillar proteins degradation from bovine viaμ-calpain[J].Food Chemistry,2012,134:106-112.
[27]Kitamura S,Muroya S,Tanabe S,et al.Mechanism of production of troponin T fragments during postmortem aging of porcine muscle[J].Journal of Agricultural and Food Chemistry,2006,53:4178-4181.
[28]Zhang W G,Xiao S,Ahn D U.Protein oxidation:basic principles and implications for meat quality[J].Critical Reviews in Food Science and Nutrition,2013,53(11):1191-1201.
[29]Furst D,Osborn M,Weber K.Myogenesis in the mouse embryo:Differential onset of expression of myogenic proteins and the involvement of titin in myofibril assembly[J].Journal of Cell Biology,1989,109(2),517-527.
[30]Penny I F,Dransfield E.The relationship between toughness and troponin-T in conditioned beef[J].Meat Science,1979,3(4):135-138.
[2]Kerry J P,O’grady M N,Hogan S A.Past,current and potential utilisation of active and intelligent packaging systems for meat and muscle-based products:A review[J].Meat Science,2006,74:113-130.
[3]Shacter E.Quantification and significance of protein oxidation in biological samples[J].Drug Metabolism Reviews,2000,32:307-326.
[4]Vitale M,Pérez-Juan M,Lloret E,et al.Effect of aging time in vacuum on tenderness,and color and lipid stability of beef from mature cows during display in high oxygen atmosphere package[J].Meat Science,2014,96:270-277.
[5]孔保华,刁新平.冷却肉包装保鲜技术的研究进展[J].肉类研究,2008,2:54-59.
[6]Skandamis P N,Nychas G E.Preservation of fresh meat with active and modified atmosphere packaging conditions[J].International Journal of Food Microbiology,2002,79:35-45.
[7]Liu C L,Zhang Y M,Yang X M,et al.Potential mechanisms of carbon monoxide and high oxygen packaging in maintaining color stability of different bovine muscles[J].Meat Science,2014,97(2):189-196.
[8]Clausen I,Jakobsen M,Ertbjerg P,et al.Modified atmosphere packaging affects lipid oxidation,myofibrillar fragmentation index and eating quality of beef[J].Packaging Technology and Science,2009,22(2):85-96.
[9]Delles R M,Xiong Y L.The effect of protein oxidation on hydration and water-binding in pork packaged in an oxygen-enriched atmosphere[J].Meat Science,2014,97(2):181-188.
[10]Livingston M,Brewer S,Killifer J,et al.Shelf life characteristics of enhanced modified atmosphere packaged pork[J].Meat Science,2004,68(1):115-122.
[11]Huff-Lonergan E,Lonergan S M.Mechanism of water-holding capacity of meat:The role of postmortem biochemical and structural changes.Meat Science,2005,71(1):194-204.
[12]Lund M N,Heínonen M,Baron C P,et al.Protein oxidation in muscle foods:a review[J].Molecular Nutrition and Food Research,2011,55(1):83-95.
[13]Park D,Xiong Y L,Alderton A L.Concentration effects of hydroxyl radical oxidizing systems on biochemical properties of porcine muscle myofibrillar protein[J].Food Chemistry,2006,101(3):1239-1246.
[14]Gornall A G,Bardawill C J,David M M.Determination of serum proteins by means of the biuret reaction[J].Journal of Biological Chemistry,1949,177(2):751-766.
[15]Astruc T,Marinova P,Labas R,et al.Detection and localization of oxidized proteins in muscle cells by fluorescence microscopy[J].Journal of Agricultural and Food Chemistry,2007,55(23):9554-9558.
[16]Chelh I,Gatellier P,SantéLhoutellier V.Technical note:A simplified procedure for myofibril hydrophobicity determination[J].Meat Science,2006,74(4):681-684.
[17]Joo S T,Kauffman R G,Kim B C,et al.The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water-holding capacity in porcine longissimus muscle[J].Meat Science,1999,52(3):291-297.
[18]Fu Q Q,Liu R,Zhang W G,et al.Effects of different packaging systems on beef tenderness through protein modifications[J].Food and Bioprocess Technology,2015,8(3):580-588.
[19]Li Y P,Liu R,Zhang W G,et al.Effect of nitric oxide onμ?calpain activation,protein proteolysis,and protein oxidation of pork during post-mortem aging[J].Journal of Agriculture and Food Chemistry,2014,62(25):5972-5977.
[20]Stadman E R,Levine R L.Protein oxidation[J].Annals the New York Academy of Sciences,2000,899(1):191-208.
[21]Sheikh M I,Gerdes U.Interaction of phenolsulphonphtalein dyes with rabbit plasma and rabbit serum albumin[J].Archives Internationales de Physiologie et de Biochimie,1978,86:613-623.
[22]Huang Y R,Hua Y F,Qiu A Y.Soybean protein aggregation induced by lipoxygenase catalyzed linoleic acid oxidation[J].Food Research International,2006,39:240-249.
[23]Santé-Lhoutellier V,Aubry L,Gatellier P.Effect of oxidation on in vitro digestibility of skeletal muscle myofibrillar proteins[J].Journal of Agricultural and Food Chemistry,2007,55:5343-5348.
[24]Yarnpakdee S,Benjakul S,Visessanguan W,et al.Thermal properties and heat-induced aggregation of natural actomyosin extracted from goatfish(Mulloidichthys martinicus)muscle as influenced by iced storage[J].Food Hydrocolloids,2009,23:1779-1784.
[25]胡忠良.鸡胸肉肌原纤维蛋白氧化对其热诱导凝胶和理化特性的影响[D].南京:南京农业大学,2012.
[26]Xue M,Huang F,Huang M,et al.Influence of oxidation on myofibrillar proteins degradation from bovine viaμ-calpain[J].Food Chemistry,2012,134:106-112.
[27]Kitamura S,Muroya S,Tanabe S,et al.Mechanism of production of troponin T fragments during postmortem aging of porcine muscle[J].Journal of Agricultural and Food Chemistry,2006,53:4178-4181.
[28]Zhang W G,Xiao S,Ahn D U.Protein oxidation:basic principles and implications for meat quality[J].Critical Reviews in Food Science and Nutrition,2013,53(11):1191-1201.
[29]Furst D,Osborn M,Weber K.Myogenesis in the mouse embryo:Differential onset of expression of myogenic proteins and the involvement of titin in myofibril assembly[J].Journal of Cell Biology,1989,109(2),517-527.
[30]Penny I F,Dransfield E.The relationship between toughness and troponin-T in conditioned beef[J].Meat Science,1979,3(4):135-138.