ATP处理对宰后浙东白鹅肌原纤维蛋白结构与蒸煮损失率的影响
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摘要
为研究ATP处理对鹅肉骨骼肌组织肌原纤维蛋白二级结构和保水性的影响,以浙东白鹅为试验对象,探究ATP浸泡后鹅肉在成熟过程中,骨骼肌组织内能量代谢物质(ATP、ADP和AMP)的含量、肌肉组织的超微结构、肌原纤维蛋白二级结构以及鹅肉的蒸煮损失率变化。结果表明,与对照组(CK)相比,20 mmol·L~(-1)ATP处理显著促进了鹅肉组织内ATP、ADP和AMP的含量,同时促进了肌肉组织中Z线和I带的断裂。拉曼光谱分析肌原纤维蛋白二级结构含量显示,20 mmol·L~(-1)ATP处理显著促进了肌原纤维蛋白α-螺旋逐渐向无规则卷曲和β-折叠转变(P<0.001);保水性结果分析显示,与CK相比,20 mmol·L~(-1)ATP处理在成熟48~168 h有更低蒸煮损失率(P<0.001)。蛋白质二级结构和蒸煮损失率相关性分析显示,α-螺旋与蒸煮损失率呈显著正相关(r=0.92,P<0.001);β-折叠(r=-0.87,P<0.001)、β-转角(r=-0.72,P<0.001)、无规则卷曲(r=-0.85,P<0.001)与蒸煮损失率均呈显著负相关。本研究为探究ATP处理对肌肉保水性的影响提供了理论支撑和新思路。
In order to evaluate the effect of Adenosine triphosphate( ATP) treatments on the structure of myofibrillar proteins and water holding capacity of goose skeletal muscle,the metabolism of energy level( ATP,ADP and AMP),the ultrastructure of muscle tissue,the content of sestructure content of myofibrillar proteins and the change of cooking loss were investigated during the postmortem aging. The results of metabolism showed that 20 mmol·L~(-1) ATP treatments significantly increased the content of ATP,ADP and AMP in goose tissue compared with the control,which accelerated the rupture of myofibrils in Z-line and I-band. Secondary structure content of myofibrillar proteins showed that 20 mmol·L~(-1) ATP treatments significantly increased the content of random coil( P < 0. 001) and β-sheets( P < 0. 001),and accompanied the decrease of α-helix( P < 0. 001) using Raman spectroscopy. It implied that 20 mmol·L~(-1) ATP treatments accelerated the gradually transformation of α-helix into random coil and β-sheets. The results of water holding capacity showed that compared with control,20 mmol·L~(-1) ATP treatments had a lower cooking loss( P < 0. 001) from48 to 168 h during the postmortem aging. The correlation between secondary structure of proteins and cooking loss further demonstrated that cooking loss was positively significant correlated with α-helical( r = 0. 92,P < 0. 001),and was negatively significant correlated with β-sheet( r =-0. 87,P < 0. 001),β-turn( r =-0. 72,P < 0. 001) and random coil( r =-0. 85,P < 0. 001). This study provided theoretical evidence for exploring the effect of ATP on the water hold capacity of goose skeletal muscle and gave new ideas to the goose processing industry.
In order to evaluate the effect of Adenosine triphosphate( ATP) treatments on the structure of myofibrillar proteins and water holding capacity of goose skeletal muscle,the metabolism of energy level( ATP,ADP and AMP),the ultrastructure of muscle tissue,the content of sestructure content of myofibrillar proteins and the change of cooking loss were investigated during the postmortem aging. The results of metabolism showed that 20 mmol·L~(-1) ATP treatments significantly increased the content of ATP,ADP and AMP in goose tissue compared with the control,which accelerated the rupture of myofibrils in Z-line and I-band. Secondary structure content of myofibrillar proteins showed that 20 mmol·L~(-1) ATP treatments significantly increased the content of random coil( P < 0. 001) and β-sheets( P < 0. 001),and accompanied the decrease of α-helix( P < 0. 001) using Raman spectroscopy. It implied that 20 mmol·L~(-1) ATP treatments accelerated the gradually transformation of α-helix into random coil and β-sheets. The results of water holding capacity showed that compared with control,20 mmol·L~(-1) ATP treatments had a lower cooking loss( P < 0. 001) from48 to 168 h during the postmortem aging. The correlation between secondary structure of proteins and cooking loss further demonstrated that cooking loss was positively significant correlated with α-helical( r = 0. 92,P < 0. 001),and was negatively significant correlated with β-sheet( r =-0. 87,P < 0. 001),β-turn( r =-0. 72,P < 0. 001) and random coil( r =-0. 85,P < 0. 001). This study provided theoretical evidence for exploring the effect of ATP on the water hold capacity of goose skeletal muscle and gave new ideas to the goose processing industry.
引文
[1]Huff-Lonergan E,Lonergan S M.Mechanisms of water-holding capacity of meat:the role of postmortem biochemical and structural changes[J].Meat Science,2005,71(1):194-204
[2]Qiu N.Effects of chemical composition,collagen and myoglobin content,sarcomere length,and water-holding capacity on the tenderness,and color of emu meat[D].Texas:Texas Tech University,1998
[3]Kristensen L,Purslow P P.The effect of ageing on the water-holding capacity of pork:role of cytoskeletal proteins[J].Meat Science,2001,58(1):17-23
[4]Frylinck Strydom P E,Webb E C,Du T.Effect of South African beef production systems on post-mortem muscle energy status and meat quality[J].Meat Science,2013,93(4):827-837
[5]Okitani A,Ichinose N,Miki K O Z A,Yamanaka K,Migita K,Matsuishi M.AMP and IMP dissociate actomyosin into actin and myosin[J].Bioscience Biotechnology&Biochemistry,2008,72(8):2005-2011
[6]Zhou C Y,Wang Y,Pan D,Sun Y Y,Cao J X.The effect of Cytochalasin B and Jasplakinolide on depolymerization of actin filaments in goose muscles during postmortem conditioning[J].Food Research International,2016,90:1-7
[7]Bandorowicz-Pikua J,Wrzosek A,Danieluk M,Pikula S,Buchet R.ATP-binding site of annexin VI characterized by photochemical release of nucleotide and infrared difference spectroscopy[J].Biochemical and Biophysical Research Communications,1999,263(3):775-779
[8]Berhe D T,Engelsen S B,Hviid M S,Lametsch R.Raman spectroscopic study of effect of the cooking temperature and time on meat proteins[J].Food Research International,2014,66(66):123-131
[9]Beattie R J,Bell S J,Farmer L J,Moss B W,Patterson D.Preliminary investigation of the application of Raman spectroscopy to the prediction of the sensory quality of beef silverside[J].Meat Science,2004,66(4):903-913
[10]Sun W,Zhao Q,Zhao M,Yang B,Cui C,Ren J.Structural evaluation of myofibrillar proteins during processing of Cantonese sausage by Raman spectroscopy[J].Journal of Agricultural and Food Chemistry,2011,59(20):11070-11077
[11]Aliani M,Farmer L J,Kennedy J T,Moss B W,Gordon A.Postslaughter changes in ATP metabolites,reducing and phosphorylated sugars in chicken meat[J].Meat Science,2013,94(1):55-62
[12]Huang M,Huang F,Xue M,Xu X,Zhou G.The effect of active caspase-3 on degradation of chicken myofibrillar proteins and structure of myofibrils[J].Food Chemistry,2011,128(1):22-27
[13]周昌瑜,楼宵玮,杜筱婧,杨阳,曹锦轩,潘道东,孙杨赢.氯化钙注射对鹅肉成熟机制及品质影响的研究[J].现代食品科技,2016,32(10):151-159
[14]Sch9nfeldt H C,Strydom P E.Effect of age and cut on cooking loss,juiciness and flavour of South African beef[J].Meat Science,2011,87(3):180-190
[15]Henckel P,Karlsson A,Jensen M T,Oksbjerg N,Petersen J S.Metabolic conditions in porcine longissimus muscle immediately preslaughter and its influence on peri-and post mortem energy metabolism[J].Meat Science,2002,62(2):145-155
[16]曹锦轩.宰后牛肉成熟过程中肌细胞死亡生理研究[D].南京:南京农业大学,2010
[17]Lametsch R,Roepstorff P,Bendixen E.Identification of protein degradation during post-mortem storage of pig meat[J].Journal of Agricultural and Food Chemistry,2002,50(20):5508-5512
[18]Taylor R G,Geesink G H,Thompson V F,Koohmaraie M,Goll DE.Is Z-disk degradation responsible for postmortem tenderization?[J].Journal of Animal Science,1995,73(5):1351-1367
[19]Goll D E,Thompson V F,Taylor R G,Ouali A.The calpain system and skeletal muscle growth[J].Canadian Journal of Animal Science,1998,78:503-512
[20]Shen Q W,Swartz D R.Influence of salt and pyrophosphate on bovine fast and slow myosin S1 dissociation from actin[J].Meat Science,2010,84(3):364-370
[21]Becker E W.The roles of ATP in the dynamics of the actin filaments of the cytoskeleton[J].Biological Chemistry,2006,387(4):401-406
[22]Herrero A M,Carmona P,García M L,Solas M T,Careche M.Ultrastructural changes and structure and mobility of myowater in frozen-stored hake(Merluccius merluccius L.)muscle:relationship with functionality and texture[J].Journal of Agricultural and Food Chemistry,2005,53(7):2558-2566
[23]Herrero A M,Carmona P,Careche M.Raman spectroscopic study of structural changes in hake(Merluccius merluccius L.)muscle proteins during frozen storage[J].Journal of Agricultural and Food Chemistry,2004,52(8):2147-2153
[24]Wu Z,Bertram H C,Kohler A,B9cker U,Ofstad R,Andersen HJ.Influence of aging and salting on protein secondary structures and water distribution in uncooked and cooked pork.A combined FT-IRmicrospectroscopy and 1H NMR relaxometry study[J].Journal of Agricultural and Food Chemistry,2006,54(22):8589-8597
[25]Beattie J R,Bell S E,Borggaard C,Moss B W.Preliminary investigations on the effects of ageing and cooking on the Raman spectra of porcine longissimus dorsi[J].Meat Science,2008,80(4):1205-1211
[26]Beattie R J,Bell S J,Farmer L J,Moss B W,Patterson D.Preliminary investigation of the application of Raman spectroscopy to the prediction of the sensory quality of beef silverside[J].Meat Science,2004,66(4):903-913
[27]Colaianni S E M,Nielsen O F.Low-frequency Raman spectroscopy[J].Journal of Molecular Structure,1995,347:267-283
[28]Kim Y H B,Stuart A,Nygaard G,Rosenvold K.High pre rigor temperature limits the ageing potential of beef that is not completely overcome by electrical stimulation and muscle restraining[J].Meat Science,2012,91(1):62-68
[29]Suliman G M,Hussein E O S,Al-Owaimer A N.Improving mature camel-meat quality characteristics with calcium chloride injection[J].Journal of Camel Practice and Research,2013,20(1):53-57
[30]Klinhom P,Klinhom J,Senapa J,Methawiwat S.Improving the quality of citric acid and calcium chloride marinated culled cow meat[J].International Food Research Journal,2015,22(4):1410-1416
[31]Bertram H C,Kohler A,B9cker U,Ofstad R,Andersen H J.Heatinduced changes in myofibrillar protein structures and myowater of two pork qualities.A combined FT-IR spectroscopy and low-field NMR relaxometry study[J].Journal of Agricultural and Food Chemistry,2006,54(5):1740-1746
[2]Qiu N.Effects of chemical composition,collagen and myoglobin content,sarcomere length,and water-holding capacity on the tenderness,and color of emu meat[D].Texas:Texas Tech University,1998
[3]Kristensen L,Purslow P P.The effect of ageing on the water-holding capacity of pork:role of cytoskeletal proteins[J].Meat Science,2001,58(1):17-23
[4]Frylinck Strydom P E,Webb E C,Du T.Effect of South African beef production systems on post-mortem muscle energy status and meat quality[J].Meat Science,2013,93(4):827-837
[5]Okitani A,Ichinose N,Miki K O Z A,Yamanaka K,Migita K,Matsuishi M.AMP and IMP dissociate actomyosin into actin and myosin[J].Bioscience Biotechnology&Biochemistry,2008,72(8):2005-2011
[6]Zhou C Y,Wang Y,Pan D,Sun Y Y,Cao J X.The effect of Cytochalasin B and Jasplakinolide on depolymerization of actin filaments in goose muscles during postmortem conditioning[J].Food Research International,2016,90:1-7
[7]Bandorowicz-Pikua J,Wrzosek A,Danieluk M,Pikula S,Buchet R.ATP-binding site of annexin VI characterized by photochemical release of nucleotide and infrared difference spectroscopy[J].Biochemical and Biophysical Research Communications,1999,263(3):775-779
[8]Berhe D T,Engelsen S B,Hviid M S,Lametsch R.Raman spectroscopic study of effect of the cooking temperature and time on meat proteins[J].Food Research International,2014,66(66):123-131
[9]Beattie R J,Bell S J,Farmer L J,Moss B W,Patterson D.Preliminary investigation of the application of Raman spectroscopy to the prediction of the sensory quality of beef silverside[J].Meat Science,2004,66(4):903-913
[10]Sun W,Zhao Q,Zhao M,Yang B,Cui C,Ren J.Structural evaluation of myofibrillar proteins during processing of Cantonese sausage by Raman spectroscopy[J].Journal of Agricultural and Food Chemistry,2011,59(20):11070-11077
[11]Aliani M,Farmer L J,Kennedy J T,Moss B W,Gordon A.Postslaughter changes in ATP metabolites,reducing and phosphorylated sugars in chicken meat[J].Meat Science,2013,94(1):55-62
[12]Huang M,Huang F,Xue M,Xu X,Zhou G.The effect of active caspase-3 on degradation of chicken myofibrillar proteins and structure of myofibrils[J].Food Chemistry,2011,128(1):22-27
[13]周昌瑜,楼宵玮,杜筱婧,杨阳,曹锦轩,潘道东,孙杨赢.氯化钙注射对鹅肉成熟机制及品质影响的研究[J].现代食品科技,2016,32(10):151-159
[14]Sch9nfeldt H C,Strydom P E.Effect of age and cut on cooking loss,juiciness and flavour of South African beef[J].Meat Science,2011,87(3):180-190
[15]Henckel P,Karlsson A,Jensen M T,Oksbjerg N,Petersen J S.Metabolic conditions in porcine longissimus muscle immediately preslaughter and its influence on peri-and post mortem energy metabolism[J].Meat Science,2002,62(2):145-155
[16]曹锦轩.宰后牛肉成熟过程中肌细胞死亡生理研究[D].南京:南京农业大学,2010
[17]Lametsch R,Roepstorff P,Bendixen E.Identification of protein degradation during post-mortem storage of pig meat[J].Journal of Agricultural and Food Chemistry,2002,50(20):5508-5512
[18]Taylor R G,Geesink G H,Thompson V F,Koohmaraie M,Goll DE.Is Z-disk degradation responsible for postmortem tenderization?[J].Journal of Animal Science,1995,73(5):1351-1367
[19]Goll D E,Thompson V F,Taylor R G,Ouali A.The calpain system and skeletal muscle growth[J].Canadian Journal of Animal Science,1998,78:503-512
[20]Shen Q W,Swartz D R.Influence of salt and pyrophosphate on bovine fast and slow myosin S1 dissociation from actin[J].Meat Science,2010,84(3):364-370
[21]Becker E W.The roles of ATP in the dynamics of the actin filaments of the cytoskeleton[J].Biological Chemistry,2006,387(4):401-406
[22]Herrero A M,Carmona P,García M L,Solas M T,Careche M.Ultrastructural changes and structure and mobility of myowater in frozen-stored hake(Merluccius merluccius L.)muscle:relationship with functionality and texture[J].Journal of Agricultural and Food Chemistry,2005,53(7):2558-2566
[23]Herrero A M,Carmona P,Careche M.Raman spectroscopic study of structural changes in hake(Merluccius merluccius L.)muscle proteins during frozen storage[J].Journal of Agricultural and Food Chemistry,2004,52(8):2147-2153
[24]Wu Z,Bertram H C,Kohler A,B9cker U,Ofstad R,Andersen HJ.Influence of aging and salting on protein secondary structures and water distribution in uncooked and cooked pork.A combined FT-IRmicrospectroscopy and 1H NMR relaxometry study[J].Journal of Agricultural and Food Chemistry,2006,54(22):8589-8597
[25]Beattie J R,Bell S E,Borggaard C,Moss B W.Preliminary investigations on the effects of ageing and cooking on the Raman spectra of porcine longissimus dorsi[J].Meat Science,2008,80(4):1205-1211
[26]Beattie R J,Bell S J,Farmer L J,Moss B W,Patterson D.Preliminary investigation of the application of Raman spectroscopy to the prediction of the sensory quality of beef silverside[J].Meat Science,2004,66(4):903-913
[27]Colaianni S E M,Nielsen O F.Low-frequency Raman spectroscopy[J].Journal of Molecular Structure,1995,347:267-283
[28]Kim Y H B,Stuart A,Nygaard G,Rosenvold K.High pre rigor temperature limits the ageing potential of beef that is not completely overcome by electrical stimulation and muscle restraining[J].Meat Science,2012,91(1):62-68
[29]Suliman G M,Hussein E O S,Al-Owaimer A N.Improving mature camel-meat quality characteristics with calcium chloride injection[J].Journal of Camel Practice and Research,2013,20(1):53-57
[30]Klinhom P,Klinhom J,Senapa J,Methawiwat S.Improving the quality of citric acid and calcium chloride marinated culled cow meat[J].International Food Research Journal,2015,22(4):1410-1416
[31]Bertram H C,Kohler A,B9cker U,Ofstad R,Andersen H J.Heatinduced changes in myofibrillar protein structures and myowater of two pork qualities.A combined FT-IR spectroscopy and low-field NMR relaxometry study[J].Journal of Agricultural and Food Chemistry,2006,54(5):1740-1746