预热处理大豆蛋白对鲤鱼肌原纤维蛋白凝胶和流变学特性的影响
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摘要
以鲤鱼肌原纤维蛋白(myofibrillar protein isolate,MPI)为研究对象,研究经过预热处理的大豆分离蛋白(soy protein isolate,SPI)对MPI凝胶和流变学特性的影响。SPI在90℃热处理0(天然SPI)、30 min和180 min,分别与MPI以不同的比例(0∶1、1∶1、1∶2、1∶3、1∶4)混合,所有溶液总蛋白质量浓度均为40 mg/mL。结果表明,经过预热处理的SPI与MPI混合后其凝胶硬度、弹性、白度和持水性显著高于天然SPI与MPI混合所形成的蛋白凝胶(P<0.05),且预热处理时间越长的大豆蛋白(180 min)与短时间处理(30 min)相比增加得更为明显(P<0.05)。此外,随着SPI-MPI复配1∶1～1∶4,混合蛋白凝胶硬度、弹性、白度和持水性显著增大(P<0.05)。流变学研究表明,SPI添加到MPI溶液中能增加蛋白变性温度,而经过预热处理SPI能够显著地提高储能模量(G’)。热稳定性结果表明,MPI中添加天然SPI能够显著降低T_(max3)(P<0.05)而对T_(max1)和T_(max2)无影响(P>0.05);当SPI经过热处理后添加到MPI中能够显著降低T_(max1)(P<0.05)而提高T_(max3)(P<0.05)。总之,与未经预热处理的SPI相比,经过预热处理后的SPI添加到MPI中能够改善蛋白凝胶特性和流变学特性。
The aim of this study was to investigate the impact of preheated soy protein isolate(SPI) on the gelation and rheological properties of heat-induced myofibrillar protein isolate(MPI) extracted from common carp muscle. SPI heated at 90 ℃ for 0, 30 and 180 min were incorporated into MPI(0:1, 1:1, 1:2, 1:3, and 1:4), and protein content in the mixture solutions was kept at 40 mg/mL. Results showed that the gel hardness, springiness, whiteness, and water-holding capacity of MPI with preheated SPI were significantly higher than those with native SPI(P < 0.05), and a greater increase was observed with longer(180 min) versus shorter(30 min) heating time(P < 0.05). In addition, the hardness, springiness, whiteness and water-holding capacity of the mixed protein gels increased significantly with decreasing SPI/MPI ratio from 1:1 to 1:4(P < 0.05). The rheological properties suggested that protein denaturation temperature increased after the addition of SPI,and preheated SPI significantly increased protein storage modulus(G'). The results of thermal stability suggested that the maximum transition temperature T_(max3) was significantly reduced with the addition of native SPI to MPI(P < 0.05) while the T_(max1) and T_(max2) were not affected(P > 0.05). However, the addition of preheated SPI to MPI significantly reduced the T_(max1) and increased the T_(max3)(P < 0.05). In short, compared with native SPI, preheated SPI can improve the gelling and rheological properties of myofibrillar proteins.
The aim of this study was to investigate the impact of preheated soy protein isolate(SPI) on the gelation and rheological properties of heat-induced myofibrillar protein isolate(MPI) extracted from common carp muscle. SPI heated at 90 ℃ for 0, 30 and 180 min were incorporated into MPI(0:1, 1:1, 1:2, 1:3, and 1:4), and protein content in the mixture solutions was kept at 40 mg/mL. Results showed that the gel hardness, springiness, whiteness, and water-holding capacity of MPI with preheated SPI were significantly higher than those with native SPI(P < 0.05), and a greater increase was observed with longer(180 min) versus shorter(30 min) heating time(P < 0.05). In addition, the hardness, springiness, whiteness and water-holding capacity of the mixed protein gels increased significantly with decreasing SPI/MPI ratio from 1:1 to 1:4(P < 0.05). The rheological properties suggested that protein denaturation temperature increased after the addition of SPI,and preheated SPI significantly increased protein storage modulus(G'). The results of thermal stability suggested that the maximum transition temperature T_(max3) was significantly reduced with the addition of native SPI to MPI(P < 0.05) while the T_(max1) and T_(max2) were not affected(P > 0.05). However, the addition of preheated SPI to MPI significantly reduced the T_(max1) and increased the T_(max3)(P < 0.05). In short, compared with native SPI, preheated SPI can improve the gelling and rheological properties of myofibrillar proteins.
引文
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[16]CHIN K B,GO M Y,XIONG Y L.Konjac flour improved textural and water retention properties of transglutaminase-mediated,heatinduced porcine myofibrillar protein gel:effect of salt level and transglutaminase incubation[J].Meat Science,2009,81(3):565-572.DOI:10.1016/j.meatsci.2008.10.012.
[17]BUAMARD N,BENJAKUL S.Improvement of gel properties of sardine(Sardinella albella)surimi using coconut husk extracts[J].Food Hydrocolloids,2015,51:146-155.DOI:10.1016/j.foodhyd.2015.05.011.
[18]PARK J W.Functional protein additives in surimi gels[J].Journal of Food Science,1994,59(3):525-527.DOI:10.1111/j.1365-2621.1994.tb05554.x.
[19]SALVADOR P,TOLDRàM,SAGUER E,et al.Microstructurefunction relationships of heat-induced gels of porcine haemoglobin[J].Food Hydrocolloids,2009,23(7):1654-1659.DOI:10.1016/j.foodhyd.2008.12.003.
[20]LIU Q,GENG R,ZHAO J Y,et al.Structural and gel textural properties of soy protein isolate when subjected to extreme acid pH-shifting and mild heating processes[J].Journal of Agricultural&Food Chemistry,2015,63(19):4853-4861.DOI:10.1021/acs.jafc.5b01331.
[21]O’KANE F E,HAPPE R P,VEREIJKEN J M,et al.Heat-induced gelation of pea legumin:comparison with soybean glycinin[J].Journal of Agricultural&Food Chemistry,2004,52(16):5071-5078.DOI:10.1021/jf035215h.
[22]EGELANDSDAL B,FRETHEIM K,SAMEJIMA K.Dynamic rheological measurements on heat-induced myosin gels:effect of ionic strength,protein concentration and addition of adenosine triphosphate or pyrophosphate[J].Journal of the Science of Food&Agriculture,2010,37(9):915-926.DOI:10.1002/jsfa.2740370914.
[23]SAEED S,FAWTHROP S A,HOWELL N K.Electron spin resonance(ESR)study on free radical transfer in fish lipid-protein interaction[J].Journal of the Science of Food and Agriculture,1999,79(13):1809-1816.DOI:10.1111/anae.13846.
[24]NIU H L,XIA X F,WANG C,et al.Thermal stability and gel quality of myofibrillar protein as affected by soy protein isolates subjected to an acidic pH and mild heating[J].Food Chemistry,2018,242:188-195.DOI:10.1016/j.foodchem.2017.09.055.
[25]SUN J,LI X,XU X L,et al.Influence of various levels of flaxseed gum addition on the water-holding capacities of heat-induced porcine myofibrillar protein[J].Journal of Food Science,2011,76(3):C472-C478.DOI:10.1111/j.1750-3841.2011.02094.x.
[26]PAN T,GUO H Y,LI Y,et al.The effects of calcium chloride on the gel properties of porcine myosin-κ-carrageenan mixtures[J].Food Hydrocolloids,2017,63:467-477.DOI:10.1016/j.foodhyd.2016.09.026.
[27]LIU Q,CHEN Q,KONG B H,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:10.116/j.lwt.2014.02.023.
[28]DAMODARAN S.食品化学[M].江波,杨瑞金,译.北京:中国轻工业出版社,2013:903-904.
[29]EGELANDSDAL B,FRETHEIM K,SAMEJIMA K.Dynamic rheological measurements on heat-induced myosin gels:effect of ionic strength,protein concentration and addition of adenosine triphosphate or pyrophosphate[J].Journal of the Science of Food&Agriculture,1986,37(9):915-926.
[30]LIU G,XIONG Y L.Thermal transitions and dynamic gelling properties of oxidatively modified myosin,beta-lactoglobulin,soy7S globulin and their mixtures[J].Journal of the Science of Food&Agriculture,2000,80(12):1728-1734.DOI:10.1002/1097-0010(20000915)80:123.0.CO;2-A.
[31]WU W,ZHANG C M,KONG X Z,et al.Oxidative modification of soy protein by peroxyl radicals[J].Food Chemistry,2009,116(1):295-301.DOI:10.1016/j.foodchem.2009.02.049.
[32]NARINE S S,MARANGONI A G.Relating structure of fat crystal networks to mechanical properties:a review[J].Food Research International,1999,32(4):227-248.DOI:10.1016/S0963-9969(99)00078-2.
[33]FITZSIMONS S M,MULVIHILL D M,MORRIS E R.Denaturation and aggregation processes in thermal gelation of whey proteins resolved by differential scanning calorimetry[J].Food Hydrocolloids,2007,21(4):638-644.DOI:10.1016/j.foodhyd.2006.07.007.
[34]RAMIREZ-SUAREZ J C,ADDO K,XIONG Y L.Gelation of mixed myofibrillar/wheat gluten proteins treated with microbial transglutaminase[J].Food Research International,2005,38(10):1143-1149.DOI:10.1016/j.foodres.2005.04.004.
[2]PIETRASIK Z,LI-CHAN E C Y.Binding and textural properties of beef gels as affected by protein,κ-carrageenan and microbial transglutaminase addition[J].Food Research International,2002,35(1):91-98.DOI:10.1016/s0963-9969(01)00123-5.
[3]MOLINA E,PAPADOPOULOU A,LEDWARD D A.Emulsifying properties of high pressure treated soy protein isolate and 7S and 11Sglobulins[J].Food Hydrocolloids,2001,15(3):263-269.DOI:10.1016/s0268-005x(01)00023-6.
[4]HUA Y,CUI S W,WANG Q,et al.Heat induced gelling properties of soy protein isolates prepared from different defatted soybean flours[J].Food Research International,2005,38(4):377-385.DOI:10.1016/j.foodres.2004.10.006.
[5]吴超.大豆蛋白凝胶结构与非网络蛋白扩散行为或网络蛋白性质关系的研究[D].无锡:江南大学,2017.
[6]FEINER G,FEINER G.Meat products handbook:practical science and technology[M].Abington:Woodhead Publishing,2006:10-15.
[7]PENG I C,DAYTON W R,QUASS D W,et al.Studies on the subunits involved in the interaction of soybean 11S protein and myosin[J].Journal of Food Science,1982,47(6):1984-1990.DOI:10.1111/j.1365-2621.1982.tb12927.x.
[8]PENG I C,NIELSEN S S.Protein-protein interactions between soybean beta-conglycinin(B1-B6)and myosin[J].Journal of Food Science,1986,51(3):588-590.DOI:10.1111/j.1365-2621.1986.tb13886.x.
[9]FENG J,XIONG Y L.Interaction of myofibrillar and preheated soy proteins[J].Journal of Food Science,2010,67(8):2851-2856.DOI:10.1111/j.1365-2621.2002.tb08827.x.
[10]FENG J,XIONG Y L.Interaction and functionality of mixed myofibrillar and enzyme-hydrolyzed soy proteins[J].Journal of Food Science,2003,68(3):803-809.DOI:10.1111/j.1365-2621.2003.tb08246.x.
[11]曹连鹏.大豆蛋白冷凝胶的流变特性及分形结构分析[D].杭州:浙江工商大学,2015.
[12]卢岩.适度氧化改善大豆分离蛋白功能特性及其与肌原纤维蛋白互作的研究[D].哈尔滨:东北农业大学,2015.
[13]耿蕊.pH偏移结合温和热处理对大豆分离蛋白结构及功能性的影响及其与肌原纤维蛋白的互作[D].哈尔滨:东北农业大学,2015.
[14]NIU H L,LI Y,HAN J C,et al.Gelation and rheological properties of myofibrillar proteins influenced by the addition of soybean protein isolates subjected to an acidic pH treatment combined with a mild heating[J].Food Hydrocolloids,2017,70:269-276.DOI:10.1016/j.foodhyd.2017.04.001.
[15]JIANG J,XIONG Y L.Extreme pH treatments enhance the structure-reinforcement role of soy protein isolate and its emulsions in pork myofibrillar protein gels in the presence of microbial transglutaminase[J].Meat Science,2013,93(3):469-476.DOI:10.1016/j.meatsci.2012.11.002.
[16]CHIN K B,GO M Y,XIONG Y L.Konjac flour improved textural and water retention properties of transglutaminase-mediated,heatinduced porcine myofibrillar protein gel:effect of salt level and transglutaminase incubation[J].Meat Science,2009,81(3):565-572.DOI:10.1016/j.meatsci.2008.10.012.
[17]BUAMARD N,BENJAKUL S.Improvement of gel properties of sardine(Sardinella albella)surimi using coconut husk extracts[J].Food Hydrocolloids,2015,51:146-155.DOI:10.1016/j.foodhyd.2015.05.011.
[18]PARK J W.Functional protein additives in surimi gels[J].Journal of Food Science,1994,59(3):525-527.DOI:10.1111/j.1365-2621.1994.tb05554.x.
[19]SALVADOR P,TOLDRàM,SAGUER E,et al.Microstructurefunction relationships of heat-induced gels of porcine haemoglobin[J].Food Hydrocolloids,2009,23(7):1654-1659.DOI:10.1016/j.foodhyd.2008.12.003.
[20]LIU Q,GENG R,ZHAO J Y,et al.Structural and gel textural properties of soy protein isolate when subjected to extreme acid pH-shifting and mild heating processes[J].Journal of Agricultural&Food Chemistry,2015,63(19):4853-4861.DOI:10.1021/acs.jafc.5b01331.
[21]O’KANE F E,HAPPE R P,VEREIJKEN J M,et al.Heat-induced gelation of pea legumin:comparison with soybean glycinin[J].Journal of Agricultural&Food Chemistry,2004,52(16):5071-5078.DOI:10.1021/jf035215h.
[22]EGELANDSDAL B,FRETHEIM K,SAMEJIMA K.Dynamic rheological measurements on heat-induced myosin gels:effect of ionic strength,protein concentration and addition of adenosine triphosphate or pyrophosphate[J].Journal of the Science of Food&Agriculture,2010,37(9):915-926.DOI:10.1002/jsfa.2740370914.
[23]SAEED S,FAWTHROP S A,HOWELL N K.Electron spin resonance(ESR)study on free radical transfer in fish lipid-protein interaction[J].Journal of the Science of Food and Agriculture,1999,79(13):1809-1816.DOI:10.1111/anae.13846.
[24]NIU H L,XIA X F,WANG C,et al.Thermal stability and gel quality of myofibrillar protein as affected by soy protein isolates subjected to an acidic pH and mild heating[J].Food Chemistry,2018,242:188-195.DOI:10.1016/j.foodchem.2017.09.055.
[25]SUN J,LI X,XU X L,et al.Influence of various levels of flaxseed gum addition on the water-holding capacities of heat-induced porcine myofibrillar protein[J].Journal of Food Science,2011,76(3):C472-C478.DOI:10.1111/j.1750-3841.2011.02094.x.
[26]PAN T,GUO H Y,LI Y,et al.The effects of calcium chloride on the gel properties of porcine myosin-κ-carrageenan mixtures[J].Food Hydrocolloids,2017,63:467-477.DOI:10.1016/j.foodhyd.2016.09.026.
[27]LIU Q,CHEN Q,KONG B H,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:10.116/j.lwt.2014.02.023.
[28]DAMODARAN S.食品化学[M].江波,杨瑞金,译.北京:中国轻工业出版社,2013:903-904.
[29]EGELANDSDAL B,FRETHEIM K,SAMEJIMA K.Dynamic rheological measurements on heat-induced myosin gels:effect of ionic strength,protein concentration and addition of adenosine triphosphate or pyrophosphate[J].Journal of the Science of Food&Agriculture,1986,37(9):915-926.
[30]LIU G,XIONG Y L.Thermal transitions and dynamic gelling properties of oxidatively modified myosin,beta-lactoglobulin,soy7S globulin and their mixtures[J].Journal of the Science of Food&Agriculture,2000,80(12):1728-1734.DOI:10.1002/1097-0010(20000915)80:123.0.CO;2-A.
[31]WU W,ZHANG C M,KONG X Z,et al.Oxidative modification of soy protein by peroxyl radicals[J].Food Chemistry,2009,116(1):295-301.DOI:10.1016/j.foodchem.2009.02.049.
[32]NARINE S S,MARANGONI A G.Relating structure of fat crystal networks to mechanical properties:a review[J].Food Research International,1999,32(4):227-248.DOI:10.1016/S0963-9969(99)00078-2.
[33]FITZSIMONS S M,MULVIHILL D M,MORRIS E R.Denaturation and aggregation processes in thermal gelation of whey proteins resolved by differential scanning calorimetry[J].Food Hydrocolloids,2007,21(4):638-644.DOI:10.1016/j.foodhyd.2006.07.007.
[34]RAMIREZ-SUAREZ J C,ADDO K,XIONG Y L.Gelation of mixed myofibrillar/wheat gluten proteins treated with microbial transglutaminase[J].Food Research International,2005,38(10):1143-1149.DOI:10.1016/j.foodres.2005.04.004.