冻融次数对镜鲤鱼肌原纤维蛋白功能和结构特性变化的影响
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摘要
本实验通过测定肌原纤维蛋白溶解性、乳化性、δ-电势、巯基含量、自由氨基酸含量、二聚酪氨酸含量、表面疏水性和α-螺旋含量的变化,探究反复冻融过程引起镜鲤鱼肌原纤维蛋白功能特性和结构特性的变化。结果表明:当冻融次数增加到5次时,肌原纤维蛋白的溶解度、乳化活性、乳化稳定性分别显著下降至62.85%、20.67 m~2/g、34.83%(P<0.05);在冻融过程中随着冻融次数的增加,蛋白质的δ-电势、表面疏水性和二聚酪氨酸含量不断增加,而巯基、自由氨基酸和α-螺旋含量不断下降。蛋白质的这些变化表明,冷冻-解冻循环破坏了镜鲤鱼肌原纤维蛋白的完整结构,降低了蛋白质的功能特性。
The effect of freeze-thaw cycles on the functional and structural properties of myofibrillar protein from mirror carp(Cyprinus carpio var. specularis) was investigated by measuring the changes in the emulsifying properties, solubility,δ-potential, surface hydrophobicity and content of sulfydryl, free amino acids, dityrosine, surface hydrophobicity andα-helix. The results indicated that the solubility, emulsifying activity and emulsion stability of myofibrillar protein decreased to 62.85%, 20.67 m~2/g and 34.83%, respectively after five freeze-thaw cycles(P < 0.05). The δ-potential, surface hydrophobicity and dityrosine content increased constantly with the increase of freeze-thaw cycles, while the sulfydryl,free amino acid and α-helical contents decreased gradually. These changes suggested that freeze-thaw cycles damaged the structural integrity and functional properties of fish myofibrillar protein.
The effect of freeze-thaw cycles on the functional and structural properties of myofibrillar protein from mirror carp(Cyprinus carpio var. specularis) was investigated by measuring the changes in the emulsifying properties, solubility,δ-potential, surface hydrophobicity and content of sulfydryl, free amino acids, dityrosine, surface hydrophobicity andα-helix. The results indicated that the solubility, emulsifying activity and emulsion stability of myofibrillar protein decreased to 62.85%, 20.67 m~2/g and 34.83%, respectively after five freeze-thaw cycles(P < 0.05). The δ-potential, surface hydrophobicity and dityrosine content increased constantly with the increase of freeze-thaw cycles, while the sulfydryl,free amino acid and α-helical contents decreased gradually. These changes suggested that freeze-thaw cycles damaged the structural integrity and functional properties of fish myofibrillar protein.
引文
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[5]BENJAKUL S,BAUER F.Biochemical and physicochemical changes in catfish(Silurus glanis Linne)muscle as influenced by different freeze-thaw cycles[J].Food Chemistry,2001,72(2):207-217.DOI:10.1016/S0308-8146(00)00222-3.
[6]XIONG Youling L.,NOEL D C,MOODY W G.Textural and sensory properties of low-fat beef sausages with added water and polysaccharides as affected by pH and salt[J].Journal of Food Science,1999,64(3):550-554.DOI:10.1111/j.1365-2621.1999.tb15083.x.
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[8]PEARCE K N,KINSELLA J E.Emulsifying properties of proteins:evaluation of a turbidimetric technique[J].Journal of Agricultural and Food Chemistry,1978,26(3):716-723.DOI:10.1021/jf60217a041.
[9]XIA Xiufang,KONG Baohua,LIU Qian,et al.Physicochemical change and protein oxidation in porcine longissimus dorsi as influenced by different freeze-thaw cycles[J].Meat Science,2009,83(2):239-245.DOI:10.1016/j.meatsci.2009.05.003.
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[12]DAVIES K J,DELSIGNORE M E,LIN S W.Protein damage and degradation by oxygen radicals.II.modification of amino acids[J].Journal of Biological Chemistry,1987,262(20):9902-9907.
[13]LIU Qian,LU Yan,HAN Jianchun,et al.Structure-modification by moderate oxidation in hydroxyl radical-generating systems promote the emulsifying properties of soy protein isolate[J].Food Structure,2015,6(10):21-28.DOI:10.1016/j.foostr.2015.10.001.
[14]WU Shengjun,PAN Saikun,WANG Hongbin.Effect of trehalose on Lateolabrax japonicus,myofibrillar protein during frozen storage[J].Food Chemistry,2014,160:281-285.DOI:10.1016/j.foodchem.2014.03.100.
[15]CHANARAT S,BENJAKUL S.Effect of formaldehyde on protein cross-linking and gel forming ability of surimi from lizardfish induced by microbial transglutaminase[J].Food Hydrocolloids,1951,30(2):704-711.DOI:10.1016/j.foodhyd.2012.09.001.
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[17]MALHOTRA A,COUPLAND J N.The effect of surfactants on the solubility,zeta potential,and viscosity of soy protein isolates[J].Food Hydrocolloids,2004,18(1):101-108.DOI:10.1016/S0268-005X(03)00047-X.
[18]MOHAN M,RAMACHANDRAN D,SANKAR T V.Functional properties of Rohu(Labeo rohita)proteins during iced storage[J].Food Research International,2006,39(8):847-854.DOI:10.1016/j.foodres.2006.04.003.
[19]LIU Qian,CHEN Qian,KONG Baohua,et al.The influence of superchilling and cryoprotectants on protein oxidation and structural changes in the myofibrillar proteins of common carp(Cyprinus carpio)surimi[J].LWT-Food Science and Technology,2014,57(2):603-611.DOI:10.1016/j.lwt.2014.02.023.
[20]XIONG Youling L.,AGYARE K K,ADDO K.Hydrolyzed wheat gluten suppresses transglutaminase-mediated gelation but improves emulsification of pork myofibrillar protein[J].Meat Science,2008,80(2):535-544.DOI:10.1016/j.meatsci.2008.02.005.
[21]郭延娜.加工条件和冻结对猪肉肌原纤维蛋白乳化特性的影响研究[D].南京:南京农业大学,2009:47-48.
[22]SOMPONGSE W,ITOH Y,OBATAKE A.Effect of cryoprotectants and a reducing reagent on the stability of actomyosin during ice storage[J].Fisheries Science,1996,62(1):220-221.DOI:10.2331/fishsci.62.73.
[23]BENJAKUL S,BAUER F.Biochemical and physicochemical changes in catfish(Silurus glanis,Linne)muscle as influenced by different freeze-thaw cycles[J].Food Chemistry,2001,72(2):207-217.DOI:10.1016/S0308-8146(00)00222-3.
[24]ZHANG Mingcheng,LI Fangfei,DIAO Xinping,et al.Moisture migration,microstructure damage and protein structure changes in porcine longissimus muscle as influenced by multiple freezethaw cycles[J].Meat Science,2017,133(11):10-18.DOI:10.1016/j.meatsci.2017.05.019.
[25]CAO Yungang,XIONG Youling L..Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein[J].Food Chemistry,2015,180(1):235-243.DOI:10.1016/j.foodchem.2015.02.036.
[26]JIA Guoliang,NIRASAWA S,JI Xiaohua,et al.Physicochemical changes in myofibrillar proteins extracted from pork tenderloin thawed by a high-voltage electrostatic field[J].Food Chemistry,2018,240:910-916.DOI:10.1016/j.foodchem.2017.07.138.
[27]CORTéS-RUIZ J A,PACHECO-AGUILAR R,RAMíREZ-SUáREZ J C,et al.Conformational changes in proteins recovered from jumbo squid(Dosidicus gigas)muscle through pH shift washing treatments[J].Food Chemistry,2016,196(9):769-775.DOI:10.1016/j.foodchem.2015.09.054.
[28]李侠,孙圳,杨方威,等.适宜冻结温度保持牛肉蛋白稳定性抑制水分态变[J].农业工程学报,2015,31(23):238-245.DOI:10.11975/j.issn.1002-6819.2015.23.032.
[29]李艳青.蛋白质氧化对鲤鱼蛋白结构和功能性的影响及其控制技术[D].哈尔滨:东北农业大学,2013:77.
[30]CHEN Xing,ZHOU Ruiyun,XU Xinglian,et al.Structural modification by high-pressure homogenization for improved functional properties of freeze-dried myofibrillar proteins powder[J].Food Research International,2017,100(7):193-200.DOI:10.1016/j.foodres.2017.07.007.
[31]KORZENIOWSKA M,CHEUNG I W Y,LI-CHAN E C Y.Effects of fish protein hydrolysate and freeze-thaw treatment on physicochemical and gel properties of natural actomyosin from Pacific cod[J].Food Chemistry,2013,138(2/3):1967-1975.DOI:10.1016/j.foodchem.2012.09.150.
[32]CARECHE M,COFRADES S J.CARBALLO A,et al.Emulsifying and gelation properties during freezing and frozen storage of hake,pork,and chicken actomyosins as affected by addition of formaldehyde[J].Journal of Agricultural and Food Chemistry,1998,46(3):813-819.DOI:10.1021/jf9705173.
[33]JIA Na,WANG Letian,SHAO Junhua,et al.Changes in the structural and gel properties of pork myofibrillar protein induced by catechin modification[J].Meat Science,2017,127(1):45-74.DOI:10.1016/j.meatsci.2017.01.004.
[34]LIU R,ZHAO S M,XIONG S B,et al.Role of secondary structures in the gelation of porcine myosin at different pH values[J].Meat Science,2008,80(3):632-639.DOI:10.1016/j.meatsci.2008.02.014.
[35]SUN Weizheng,ZHOU Feibai,SUN Da-Wen,et al.Effect of oxidation on the emulsifying properties of myofibrillar proteins[J].Food and Bioprocess Technology,2013,6(7):1703-1712.DOI:10.1007/s11947-012-0823-8.
[2]UTRERA M,MORCUENDE D,GANH?O R,et al.Role of phenolics extracting from Rosa canina L.on meat protein oxidation during frozen storage and beef patties processing[J].Food&Bioprocess Technology,2014,8(4):854-864.DOI:10.1007/s11947-014-1450-3.
[3]SRIKET P,BENJAKUL S,VISESS ANGUAN W,et al.Comparative studies on the effect of the freeze-thawing process on the physicochemical properties and microstructures of black tiger shrimp(Penaeus monodon)and white shrimp(Penaeus vannamei)muscle[J].Food Chemistry,2007,104(1):113-121.DOI:10.1016/j.foodchem.2006.11.004.
[4]TURHAN S,USTUN S N,BANK I.Effect of freeze-thaw cycles on total and heme iron contents of bonito(Sarda sarda)and bluefish(Pomatomus saltator)fillets[J].Journal of Food Composition&Analysis,2006,19(4):384-387.DOI:10.1016/j.jfca.2004.10.005.
[5]BENJAKUL S,BAUER F.Biochemical and physicochemical changes in catfish(Silurus glanis Linne)muscle as influenced by different freeze-thaw cycles[J].Food Chemistry,2001,72(2):207-217.DOI:10.1016/S0308-8146(00)00222-3.
[6]XIONG Youling L.,NOEL D C,MOODY W G.Textural and sensory properties of low-fat beef sausages with added water and polysaccharides as affected by pH and salt[J].Journal of Food Science,1999,64(3):550-554.DOI:10.1111/j.1365-2621.1999.tb15083.x.
[7]A?óN M C,DE LAMBALLERIE M,SPERONI F.Effect of high pressure on solubility and aggregability of calcium-added soybean proteins[J].Innovative Food Science&Emerging Technologies,2012,16(39):155-162.DOI:10.1016/j.ifset.2012.05.006.
[8]PEARCE K N,KINSELLA J E.Emulsifying properties of proteins:evaluation of a turbidimetric technique[J].Journal of Agricultural and Food Chemistry,1978,26(3):716-723.DOI:10.1021/jf60217a041.
[9]XIA Xiufang,KONG Baohua,LIU Qian,et al.Physicochemical change and protein oxidation in porcine longissimus dorsi as influenced by different freeze-thaw cycles[J].Meat Science,2009,83(2):239-245.DOI:10.1016/j.meatsci.2009.05.003.
[10]E L L M A N G L.T i s s u e s u l f h y d r y l g r o u p s[J].A r c h i v e s o f Biochemistry and Biophysics,1959,82(1):70-77.DOI:10.1016/0003-9861(59)90090-6.
[11]ADLER-NISSEN J.Determination of the degree of hydrolysis of food protein hydrolysates by trinitrobenzenesulfonic acid[J].Journal of Agricultural and Food Chemistry,1979,27(6):1256-1262.DOI:10.1021/jf60226a042.
[12]DAVIES K J,DELSIGNORE M E,LIN S W.Protein damage and degradation by oxygen radicals.II.modification of amino acids[J].Journal of Biological Chemistry,1987,262(20):9902-9907.
[13]LIU Qian,LU Yan,HAN Jianchun,et al.Structure-modification by moderate oxidation in hydroxyl radical-generating systems promote the emulsifying properties of soy protein isolate[J].Food Structure,2015,6(10):21-28.DOI:10.1016/j.foostr.2015.10.001.
[14]WU Shengjun,PAN Saikun,WANG Hongbin.Effect of trehalose on Lateolabrax japonicus,myofibrillar protein during frozen storage[J].Food Chemistry,2014,160:281-285.DOI:10.1016/j.foodchem.2014.03.100.
[15]CHANARAT S,BENJAKUL S.Effect of formaldehyde on protein cross-linking and gel forming ability of surimi from lizardfish induced by microbial transglutaminase[J].Food Hydrocolloids,1951,30(2):704-711.DOI:10.1016/j.foodhyd.2012.09.001.
[16]SRIKAR L N,REDDY G V S.Protein solubility and emulsifying capacity in frozen stored fish mince[J].Journal of the Science of Food and Agriculture,1991,55(3):447-453.DOI:10.1002/jsfa.2740550312.
[17]MALHOTRA A,COUPLAND J N.The effect of surfactants on the solubility,zeta potential,and viscosity of soy protein isolates[J].Food Hydrocolloids,2004,18(1):101-108.DOI:10.1016/S0268-005X(03)00047-X.
[18]MOHAN M,RAMACHANDRAN D,SANKAR T V.Functional properties of Rohu(Labeo rohita)proteins during iced storage[J].Food Research International,2006,39(8):847-854.DOI:10.1016/j.foodres.2006.04.003.
[19]LIU Qian,CHEN Qian,KONG Baohua,et al.The influence of superchilling and cryoprotectants on protein oxidation and structural changes in the myofibrillar proteins of common carp(Cyprinus carpio)surimi[J].LWT-Food Science and Technology,2014,57(2):603-611.DOI:10.1016/j.lwt.2014.02.023.
[20]XIONG Youling L.,AGYARE K K,ADDO K.Hydrolyzed wheat gluten suppresses transglutaminase-mediated gelation but improves emulsification of pork myofibrillar protein[J].Meat Science,2008,80(2):535-544.DOI:10.1016/j.meatsci.2008.02.005.
[21]郭延娜.加工条件和冻结对猪肉肌原纤维蛋白乳化特性的影响研究[D].南京:南京农业大学,2009:47-48.
[22]SOMPONGSE W,ITOH Y,OBATAKE A.Effect of cryoprotectants and a reducing reagent on the stability of actomyosin during ice storage[J].Fisheries Science,1996,62(1):220-221.DOI:10.2331/fishsci.62.73.
[23]BENJAKUL S,BAUER F.Biochemical and physicochemical changes in catfish(Silurus glanis,Linne)muscle as influenced by different freeze-thaw cycles[J].Food Chemistry,2001,72(2):207-217.DOI:10.1016/S0308-8146(00)00222-3.
[24]ZHANG Mingcheng,LI Fangfei,DIAO Xinping,et al.Moisture migration,microstructure damage and protein structure changes in porcine longissimus muscle as influenced by multiple freezethaw cycles[J].Meat Science,2017,133(11):10-18.DOI:10.1016/j.meatsci.2017.05.019.
[25]CAO Yungang,XIONG Youling L..Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein[J].Food Chemistry,2015,180(1):235-243.DOI:10.1016/j.foodchem.2015.02.036.
[26]JIA Guoliang,NIRASAWA S,JI Xiaohua,et al.Physicochemical changes in myofibrillar proteins extracted from pork tenderloin thawed by a high-voltage electrostatic field[J].Food Chemistry,2018,240:910-916.DOI:10.1016/j.foodchem.2017.07.138.
[27]CORTéS-RUIZ J A,PACHECO-AGUILAR R,RAMíREZ-SUáREZ J C,et al.Conformational changes in proteins recovered from jumbo squid(Dosidicus gigas)muscle through pH shift washing treatments[J].Food Chemistry,2016,196(9):769-775.DOI:10.1016/j.foodchem.2015.09.054.
[28]李侠,孙圳,杨方威,等.适宜冻结温度保持牛肉蛋白稳定性抑制水分态变[J].农业工程学报,2015,31(23):238-245.DOI:10.11975/j.issn.1002-6819.2015.23.032.
[29]李艳青.蛋白质氧化对鲤鱼蛋白结构和功能性的影响及其控制技术[D].哈尔滨:东北农业大学,2013:77.
[30]CHEN Xing,ZHOU Ruiyun,XU Xinglian,et al.Structural modification by high-pressure homogenization for improved functional properties of freeze-dried myofibrillar proteins powder[J].Food Research International,2017,100(7):193-200.DOI:10.1016/j.foodres.2017.07.007.
[31]KORZENIOWSKA M,CHEUNG I W Y,LI-CHAN E C Y.Effects of fish protein hydrolysate and freeze-thaw treatment on physicochemical and gel properties of natural actomyosin from Pacific cod[J].Food Chemistry,2013,138(2/3):1967-1975.DOI:10.1016/j.foodchem.2012.09.150.
[32]CARECHE M,COFRADES S J.CARBALLO A,et al.Emulsifying and gelation properties during freezing and frozen storage of hake,pork,and chicken actomyosins as affected by addition of formaldehyde[J].Journal of Agricultural and Food Chemistry,1998,46(3):813-819.DOI:10.1021/jf9705173.
[33]JIA Na,WANG Letian,SHAO Junhua,et al.Changes in the structural and gel properties of pork myofibrillar protein induced by catechin modification[J].Meat Science,2017,127(1):45-74.DOI:10.1016/j.meatsci.2017.01.004.
[34]LIU R,ZHAO S M,XIONG S B,et al.Role of secondary structures in the gelation of porcine myosin at different pH values[J].Meat Science,2008,80(3):632-639.DOI:10.1016/j.meatsci.2008.02.014.
[35]SUN Weizheng,ZHOU Feibai,SUN Da-Wen,et al.Effect of oxidation on the emulsifying properties of myofibrillar proteins[J].Food and Bioprocess Technology,2013,6(7):1703-1712.DOI:10.1007/s11947-012-0823-8.