生产类群、性别及包装方式对冷藏牦牛肉肌浆蛋白氧化的影响
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摘要
为了探讨冷藏条件下牦牛肉肌浆蛋白的氧化规律,本实验通过羰基含量、巯基含量、表面疏水性、紫外吸收光谱及十二烷基硫酸钠-聚丙烯酰胺凝胶电泳法研究了普通包装和真空包装方式下不同生产类群的公、母牦牛肉的肌浆蛋白氧化特性。结果表明:随冷藏时间的延长,两种包装的肌浆蛋白羰基含量呈波浪式上升趋势(P<0.05),总巯基含量下降;普通包装组表面疏水性上升(P<0.05),真空包装组表面疏水性先上升后下降;同一包装方式的不同生产类群之间肌浆蛋白羰基、总巯基含量及表面疏水性均有显著差异(P<0.05);公、母牦牛肉之间肌浆蛋白羰基、总巯基及疏水性差异均不显著(P>0.05)。两种包装的肌浆蛋白紫外吸收光谱的二阶导数光谱在冷藏第3天谱图改变最明显。随着氧化的进行,肌浆蛋白分子质量降低,所有蛋白条带均有不同程度的弱化,普通包装组肌浆蛋白降解程度大于真空包装;相同冷藏时间,2种包装方式的不同生产类群及性别的牦牛肉的肌浆蛋白紫外吸收谱图及电泳图趋于一致。该研究认为,在冷藏过程中,肌浆蛋白的蛋白氧化与包装方式、生产类群密切相关,与牦牛的性别无关。
In an effort to explore the oxidation pattern of sarcoplasmic proteins in yak meat under chilled conditions,Longissimus dorsi muscles of male and female yaks from different populations were packaged in air or vacuum and stored under chilled conditions, and the oxidation of sarcoplasmic proteins in yak meat was evaluated by measurement of carbonyl content, sulfhydryl content and hydrophobicity, UV absorption spectroscopy and sodium dodecyl sulphate polyacrylamide gel electrophoresis(SDS-PAGE). The results showed that the carbonyl content of sarcoplasmic proteins in both packaging treatments followed an increasing-decreasing-increasing trend(P < 0.05), whereas the total sulfhydryl content decreased with the prolongation of storage time. Surface hydrophobicity of air-packaged yak meat increased(P < 0.05), while that of vacuum-packaged meat revealed an initially increase and then decreased. Significant differences were observed for carbonyl content, total sulfhydryl content and surface hydrophobicity between different yak populations under the same packaging conditions(P < 0.05), but not between the genders(P > 0.05). For both packaging trearments, the most apparent change in the second-order derivative UV absorption spectra of sarcoplasmic proteins occurred on the 3 rd day of the storage.As oxidation proceeded, the molecular masss of sarcoplasmic proteins decreased, and the intensity of all protein bands declined. During storage, the degradation degree of sarcoplasmic proteins under air packaging was larger than under vacuum packaging. UV absorption spectra and SDS-PAGE patterns of sarcoplasmic proteins in both packaging treatments did not vary between populations or genders after the same storage time. From this study we concluded that sarcoplasmic protein oxidation in yak meat during cold storage was closely related to packaging methods and populations but not genders.
In an effort to explore the oxidation pattern of sarcoplasmic proteins in yak meat under chilled conditions,Longissimus dorsi muscles of male and female yaks from different populations were packaged in air or vacuum and stored under chilled conditions, and the oxidation of sarcoplasmic proteins in yak meat was evaluated by measurement of carbonyl content, sulfhydryl content and hydrophobicity, UV absorption spectroscopy and sodium dodecyl sulphate polyacrylamide gel electrophoresis(SDS-PAGE). The results showed that the carbonyl content of sarcoplasmic proteins in both packaging treatments followed an increasing-decreasing-increasing trend(P < 0.05), whereas the total sulfhydryl content decreased with the prolongation of storage time. Surface hydrophobicity of air-packaged yak meat increased(P < 0.05), while that of vacuum-packaged meat revealed an initially increase and then decreased. Significant differences were observed for carbonyl content, total sulfhydryl content and surface hydrophobicity between different yak populations under the same packaging conditions(P < 0.05), but not between the genders(P > 0.05). For both packaging trearments, the most apparent change in the second-order derivative UV absorption spectra of sarcoplasmic proteins occurred on the 3 rd day of the storage.As oxidation proceeded, the molecular masss of sarcoplasmic proteins decreased, and the intensity of all protein bands declined. During storage, the degradation degree of sarcoplasmic proteins under air packaging was larger than under vacuum packaging. UV absorption spectra and SDS-PAGE patterns of sarcoplasmic proteins in both packaging treatments did not vary between populations or genders after the same storage time. From this study we concluded that sarcoplasmic protein oxidation in yak meat during cold storage was closely related to packaging methods and populations but not genders.
引文
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[6]HUFF-LONERGAN E,LONERGAN S M.Mechanisms of waterholding capacity of meat:the role of postmortem biochemical and structural changes[J].Meat Science,2005,71(1):194-204.DOI:10.1016/j.meatsci.2005.04.022.
[7]LUND M N,LAMETSCH R,HVIID M S,et al.High-oxygen packaging atmosphere influences protein oxidation and tenderness of porcine longissimus dorsi,during chill storage[J].Meat Science,2007,77(3):295-303.DOI:10.1016/j.meatsci.2007.03.016.
[8]MORZEL M,GATELLIER P,SAYD T,et al.Chemical oxidation decreases proteolytic susceptibility of skeletal muscle myofibrillar proteins[J].Meat Science,2006,73(3):536-543.DOI:10.1016/j.meatsci.2006.02.005.
[9]TIAN J C,HAH L,YU Q L,et al.Changes in tenderness and cathepsins activity during post mortem ageing of yak meat[J].Canadian Journal of Animal Science,2013,93(3):321-328.DOI:10.4141/cjas2012-102.
[10]SCOPES R K.Isolation and properties of a basic protein from skeletalmuscle sarcoplasm[J].Biochemical Journal,1966,98(1):193-197.DOI:10.1042/bj0980193.
[11]DAI Y,MIAO J,YUAN S Z,et al.Colour and sarcoplasmic protein evaluation of pork following water bath and ohmic cooking[J].Meat Science,2013,93(4):898-905.DOI:10.1016/j.meatsci.2012.11.044.
[12]CHOI Y M,RYU Y C,LEE S H,et al.Effects of supercritical carbon dioxide treatment for sterilization purpose on meat quality of porcine longissimus dorsi muscle[J].LWT-Food Science and Technology,2008,41(2):317-322.DOI:10.1016/j.lwt.2007.02.020.
[13]BAO Y L,BOEREN S,ERTBJERG P.Myofibrillar protein oxidation affects filament charges,aggregation and water-holding[J].Meat Science,2018,135:102-108.DOI:10.1016/j.meatsci.2017.09.011.
[14]BABU?íKOVáE,KAPLáN P,LEHOTSKYJ,et al.Oxidative modification of rat cardiac mitochondrial membranes and myofibrils by hydroxyl radicals[J].General Physiology and Biophysics,2004,23(3):327-335.
[15]FUENTES V,VENTANAS J,MORCUENDE D,et al.Lipid and protein oxidation and sensory properties of vacuum-packaged drycured ham subjected to high hydrostatic pressure[J].Meat Science,2010,85(3):506-514.DOI:10.1016/j.meatsci.2010.02.024.
[16]DELLES R M,XIONG Youling L.,TRUE A D.Mild protein oxidation enhanced hydration and myofibril swelling capacity of fresh ground pork muscle packaged in high oxygen atmosphere[J].Journal of Food Science,2011,76(5):C760-C767.DOI:10.1111/j.1750-3841.2011.02195.x.
[17]闫利国,唐善虎,王柳,等.冷冻贮藏过程中氧化诱导牦牛肉肌原纤维蛋白结构的变化[J].食品科学,2015,36(24):337-342.DOI:10.7506/spkx1002-6630-201524062.
[18]TOKUR B,POLAT A.Myofibrillar and oxidation and sarcoplasmic protein degradation of thin-lipped gray mullet(Liza ramada)during refrigerated storage(4℃)[J].Journal of Muscle Foods,2010,21(1):102-118.DOI:10.1111/j.1745-4573.2009.00170.x.
[19]SOYER A,?ZALP B,DALMI?ü,et al.Effects of freezing temperature and duration of frozen storage on lipid and protein oxidation in chicken meat[J].Food Chemistry,2010,120(4):1025-1030.DOI:10.1016/j.foodchem.2009.11.042.
[20]MIYAGUCHI Y,NAGAYAMA K,TSUTSUMI M.Thermal and functional properties of porcine sarcoplasmic proteins:a comparison with some water-soluble animal proteins[J].Nihon Chikusan Gakkaiho,2000,71(4):416-424.DOI:10.2508/chikusan.71.416.
[21]马纪兵,张丽,包高良,等.包装方式对冷藏过程中牦牛肉蛋白质生化特性的影响[J].食品与发酵工业,2017,43(5):225-232.DOI:10.13995/j.cnki.11-1802/ts.201705037.
[22]SHER A.反复冻融对鸡胸肉品质的影响[D].南京:南京农业大学,2015:43-65.
[23]MARCOS B,KERRY J P,MULLEN A M.High pressure induced changes on sarcoplasmic protein fraction and quality indicators[J].Meat Science,2010,85(1):115-120.DOI:10.1016/j.meatsci.2009.12.014.
[24]GORNALL A G,BARDAWILL C J,DAVID M M.Determination of serum proteins by means of the biuret reaction[J].Journal of Biological Chemistry,1949,177:751-766.
[25]LEVINE R L,WILLIAMS J A,STADTMAN E R,et al.Carbonyl assays for determination of oxidatively modified proteins[J].Methods in Enzymology,1994,233:346-357.DOI:10.1016/s0076-6879(94)33040-9.
[26]ELLMAN G L.Tissue sulfhydryl groups[J].Archives of Biochemistry and Biophysics,1959,82(1):70-77.DOI:10.1016/0003-9861(59)90090-6.
[27]CHELH I,GATELLIER P,SANTé-LHOUTELLIER V.Technical note:a simplified procedure for myofibril hydrophobicity determination[J].Meat Science,2006,74(4):681-683.DOI:10.1016/j.meatsci.2006.05.019.
[28]LAEMMLI U K.Cleavage of structural proteins during the assembly of the head of bacteriophage T4[J].Nature,1970,227:680-685.DOI:10.1038/227680a0.
[29]CHAN J T Y,OMANA D A,BETTI M.Effect of ultimate pH and freezing on the biochemical properties of proteins in turkey breast meat[J].Food Chemistry,2011,127(1):109-117.DOI:10.1016/j.foodchem.2010.12.095.
[30]LEYGONIE C,BRITZ T J,HOFFMAN L C.Protein and lipid oxidative stability of fresh ostrich M.Iliofibularis,packaged under different modified atmospheric packaging conditions[J].Food Chemistry,2011,127(4):1659-1667.DOI:10.1016/j.foodchem.2011.02.033.
[31]SELL D R,STRAUCH C M,SHEN W,et al.2-Aminoadipic acid is a marker of protein carbonyl oxidation in the aging human skin:effects of diabetes,renal failure and sepsis[J].Biochemical Journal,2007,404(2):269-277.DOI:10.1042/bj20061645.
[32]LIU G,XIONG Youling L..Oxidatively induced chemical changes and interactions of mixed myosin,β-lactoglobulin and soy 7S globulin[J].Journal of the Science of Food and Agriculture,2000,80(11):1601-1607.DOI:10.1002/1097-0010(20000901)80:113.0.CO;2-O.
[33]BISWAS S,CHIDA A S,RAHMAN I.Redox modifications of proteinthiols:emerging roles in cell signaling[J].Biochemical Pharmacology,2006,71(5):551-564.DOI:10.1016/j.bcp.2005.10.044.
[34]EATON P.Protein thiol oxidation in health and disease:techniques for measuring disulfides and related modifications in complex protein mixtures[J].Free Radical Biology and Medicine,2006,40(11):1889-1899.DOI:10.1016/j.freeradbiomed.2005.12.037.
[35]LEELAPONGWATTANA K,BENJAKUL S,VISESSANGUAN W,et al.Physicochemical and biochemical changes in whole lizardfish(Saurida micropectoralis)muscles and fillets during frozen storage[J].Journal of Food Biochemistry,2005,29(5):547-569.DOI:10.1111/j.1745-4514.2005.00028.x.
[36]O’HAVER T C.Potential clinical applications of derivative and wavelength-modulation spectrometry[J].Clinical Chemistry,1979,25(9):1548-1553.
[37]GLAZER A N,SMITH E L.Effect of denaturation on the ultraviolet absorption spectra of proteins[J].Journal of Biological Chemistry,1960,235(1):PC43-PC44.
[38]ZHAO W,YANG R J.The effect of pulsed electric fields on the inactivation and structure of lysozyme[J].Food Chemistry,2008,110(2):334-343.DOI:10.1016/j.foodchem.2008.02.008.
[39]HUANG H G,LARSEN M R,KARLSSON A H,et al.Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences[J].Proteomics,2011,11(20):4063-4076.DOI:10.1002/pmic.201100173.
[40]王思丹,李春保,温思颖,等.禁食处理和宰后时间对鸡肉蛋白磷酸化水平的影响[J].食品科学,2013,34(19):270-274.DOI:10.7506/spkx1002-6630-201319055.
[41]GRUNE T,KLOTZ L O,GIECHE J,et al.Protein oxidation and proteolysis by the nonradical oxidants singlet oxygen or peroxynitrite[J].Free Radical Biology and Medicine,2001,30(11):1243-1253.DOI:10.1016/s0891-5849(01)00515-9.
[42]RYU Y C,CHOI Y M,KIM B C.Variations in metabolite contents and protein denaturation of the longissimus dorsi muscle in various porcine quality classifications and metabolic rates[J].Meat Science,2005,71(3):522-529.DOI:10.1016/j.meatsci.2005.04.034.
[2]AHMAD S,KHAN H,SHAHAB U,et al.Protein oxidation:an overview of metabolism of sulphur containing amino acid,cysteine[J].Frontiers in Bioscience,2017,9(1):71-87.DOI:10.2741/s474.
[3]PACIFICI R E,KONO Y,DAVIES K J.Hydrophobicity as the signal for selective degradation of hydroxyl radical-modified hemoglobin by the multicatalytic proteinase complex,proteasome[J].The Journal of Biological Chemistry,1993,268(21):15405-15411.DOI:10.1016/0005-2736(93)90126-K.
[4]XUE M,HUANG F,HUANG M,et al.Influence of oxidation on myofibrillar proteins degradation from bovine viaμ-calpain[J].Food Chemistry,2012,134(1):106-112.DOI:10.1016/j.foodchem.2012.02.072.
[5]ROWE L J,MADDOCK K R,LONERGAN S M,et al.Influence of early postmortem protein oxidation on beef quality[J].Journal of Animal Science,2004,82(3):785-793.DOI:10.1093/ansci/82.3.785.
[6]HUFF-LONERGAN E,LONERGAN S M.Mechanisms of waterholding capacity of meat:the role of postmortem biochemical and structural changes[J].Meat Science,2005,71(1):194-204.DOI:10.1016/j.meatsci.2005.04.022.
[7]LUND M N,LAMETSCH R,HVIID M S,et al.High-oxygen packaging atmosphere influences protein oxidation and tenderness of porcine longissimus dorsi,during chill storage[J].Meat Science,2007,77(3):295-303.DOI:10.1016/j.meatsci.2007.03.016.
[8]MORZEL M,GATELLIER P,SAYD T,et al.Chemical oxidation decreases proteolytic susceptibility of skeletal muscle myofibrillar proteins[J].Meat Science,2006,73(3):536-543.DOI:10.1016/j.meatsci.2006.02.005.
[9]TIAN J C,HAH L,YU Q L,et al.Changes in tenderness and cathepsins activity during post mortem ageing of yak meat[J].Canadian Journal of Animal Science,2013,93(3):321-328.DOI:10.4141/cjas2012-102.
[10]SCOPES R K.Isolation and properties of a basic protein from skeletalmuscle sarcoplasm[J].Biochemical Journal,1966,98(1):193-197.DOI:10.1042/bj0980193.
[11]DAI Y,MIAO J,YUAN S Z,et al.Colour and sarcoplasmic protein evaluation of pork following water bath and ohmic cooking[J].Meat Science,2013,93(4):898-905.DOI:10.1016/j.meatsci.2012.11.044.
[12]CHOI Y M,RYU Y C,LEE S H,et al.Effects of supercritical carbon dioxide treatment for sterilization purpose on meat quality of porcine longissimus dorsi muscle[J].LWT-Food Science and Technology,2008,41(2):317-322.DOI:10.1016/j.lwt.2007.02.020.
[13]BAO Y L,BOEREN S,ERTBJERG P.Myofibrillar protein oxidation affects filament charges,aggregation and water-holding[J].Meat Science,2018,135:102-108.DOI:10.1016/j.meatsci.2017.09.011.
[14]BABU?íKOVáE,KAPLáN P,LEHOTSKYJ,et al.Oxidative modification of rat cardiac mitochondrial membranes and myofibrils by hydroxyl radicals[J].General Physiology and Biophysics,2004,23(3):327-335.
[15]FUENTES V,VENTANAS J,MORCUENDE D,et al.Lipid and protein oxidation and sensory properties of vacuum-packaged drycured ham subjected to high hydrostatic pressure[J].Meat Science,2010,85(3):506-514.DOI:10.1016/j.meatsci.2010.02.024.
[16]DELLES R M,XIONG Youling L.,TRUE A D.Mild protein oxidation enhanced hydration and myofibril swelling capacity of fresh ground pork muscle packaged in high oxygen atmosphere[J].Journal of Food Science,2011,76(5):C760-C767.DOI:10.1111/j.1750-3841.2011.02195.x.
[17]闫利国,唐善虎,王柳,等.冷冻贮藏过程中氧化诱导牦牛肉肌原纤维蛋白结构的变化[J].食品科学,2015,36(24):337-342.DOI:10.7506/spkx1002-6630-201524062.
[18]TOKUR B,POLAT A.Myofibrillar and oxidation and sarcoplasmic protein degradation of thin-lipped gray mullet(Liza ramada)during refrigerated storage(4℃)[J].Journal of Muscle Foods,2010,21(1):102-118.DOI:10.1111/j.1745-4573.2009.00170.x.
[19]SOYER A,?ZALP B,DALMI?ü,et al.Effects of freezing temperature and duration of frozen storage on lipid and protein oxidation in chicken meat[J].Food Chemistry,2010,120(4):1025-1030.DOI:10.1016/j.foodchem.2009.11.042.
[20]MIYAGUCHI Y,NAGAYAMA K,TSUTSUMI M.Thermal and functional properties of porcine sarcoplasmic proteins:a comparison with some water-soluble animal proteins[J].Nihon Chikusan Gakkaiho,2000,71(4):416-424.DOI:10.2508/chikusan.71.416.
[21]马纪兵,张丽,包高良,等.包装方式对冷藏过程中牦牛肉蛋白质生化特性的影响[J].食品与发酵工业,2017,43(5):225-232.DOI:10.13995/j.cnki.11-1802/ts.201705037.
[22]SHER A.反复冻融对鸡胸肉品质的影响[D].南京:南京农业大学,2015:43-65.
[23]MARCOS B,KERRY J P,MULLEN A M.High pressure induced changes on sarcoplasmic protein fraction and quality indicators[J].Meat Science,2010,85(1):115-120.DOI:10.1016/j.meatsci.2009.12.014.
[24]GORNALL A G,BARDAWILL C J,DAVID M M.Determination of serum proteins by means of the biuret reaction[J].Journal of Biological Chemistry,1949,177:751-766.
[25]LEVINE R L,WILLIAMS J A,STADTMAN E R,et al.Carbonyl assays for determination of oxidatively modified proteins[J].Methods in Enzymology,1994,233:346-357.DOI:10.1016/s0076-6879(94)33040-9.
[26]ELLMAN G L.Tissue sulfhydryl groups[J].Archives of Biochemistry and Biophysics,1959,82(1):70-77.DOI:10.1016/0003-9861(59)90090-6.
[27]CHELH I,GATELLIER P,SANTé-LHOUTELLIER V.Technical note:a simplified procedure for myofibril hydrophobicity determination[J].Meat Science,2006,74(4):681-683.DOI:10.1016/j.meatsci.2006.05.019.
[28]LAEMMLI U K.Cleavage of structural proteins during the assembly of the head of bacteriophage T4[J].Nature,1970,227:680-685.DOI:10.1038/227680a0.
[29]CHAN J T Y,OMANA D A,BETTI M.Effect of ultimate pH and freezing on the biochemical properties of proteins in turkey breast meat[J].Food Chemistry,2011,127(1):109-117.DOI:10.1016/j.foodchem.2010.12.095.
[30]LEYGONIE C,BRITZ T J,HOFFMAN L C.Protein and lipid oxidative stability of fresh ostrich M.Iliofibularis,packaged under different modified atmospheric packaging conditions[J].Food Chemistry,2011,127(4):1659-1667.DOI:10.1016/j.foodchem.2011.02.033.
[31]SELL D R,STRAUCH C M,SHEN W,et al.2-Aminoadipic acid is a marker of protein carbonyl oxidation in the aging human skin:effects of diabetes,renal failure and sepsis[J].Biochemical Journal,2007,404(2):269-277.DOI:10.1042/bj20061645.
[32]LIU G,XIONG Youling L..Oxidatively induced chemical changes and interactions of mixed myosin,β-lactoglobulin and soy 7S globulin[J].Journal of the Science of Food and Agriculture,2000,80(11):1601-1607.DOI:10.1002/1097-0010(20000901)80:113.0.CO;2-O.
[33]BISWAS S,CHIDA A S,RAHMAN I.Redox modifications of proteinthiols:emerging roles in cell signaling[J].Biochemical Pharmacology,2006,71(5):551-564.DOI:10.1016/j.bcp.2005.10.044.
[34]EATON P.Protein thiol oxidation in health and disease:techniques for measuring disulfides and related modifications in complex protein mixtures[J].Free Radical Biology and Medicine,2006,40(11):1889-1899.DOI:10.1016/j.freeradbiomed.2005.12.037.
[35]LEELAPONGWATTANA K,BENJAKUL S,VISESSANGUAN W,et al.Physicochemical and biochemical changes in whole lizardfish(Saurida micropectoralis)muscles and fillets during frozen storage[J].Journal of Food Biochemistry,2005,29(5):547-569.DOI:10.1111/j.1745-4514.2005.00028.x.
[36]O’HAVER T C.Potential clinical applications of derivative and wavelength-modulation spectrometry[J].Clinical Chemistry,1979,25(9):1548-1553.
[37]GLAZER A N,SMITH E L.Effect of denaturation on the ultraviolet absorption spectra of proteins[J].Journal of Biological Chemistry,1960,235(1):PC43-PC44.
[38]ZHAO W,YANG R J.The effect of pulsed electric fields on the inactivation and structure of lysozyme[J].Food Chemistry,2008,110(2):334-343.DOI:10.1016/j.foodchem.2008.02.008.
[39]HUANG H G,LARSEN M R,KARLSSON A H,et al.Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences[J].Proteomics,2011,11(20):4063-4076.DOI:10.1002/pmic.201100173.
[40]王思丹,李春保,温思颖,等.禁食处理和宰后时间对鸡肉蛋白磷酸化水平的影响[J].食品科学,2013,34(19):270-274.DOI:10.7506/spkx1002-6630-201319055.
[41]GRUNE T,KLOTZ L O,GIECHE J,et al.Protein oxidation and proteolysis by the nonradical oxidants singlet oxygen or peroxynitrite[J].Free Radical Biology and Medicine,2001,30(11):1243-1253.DOI:10.1016/s0891-5849(01)00515-9.
[42]RYU Y C,CHOI Y M,KIM B C.Variations in metabolite contents and protein denaturation of the longissimus dorsi muscle in various porcine quality classifications and metabolic rates[J].Meat Science,2005,71(3):522-529.DOI:10.1016/j.meatsci.2005.04.034.