氧化程度对肌原纤维蛋白理化特性和凝胶水分分布的影响
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摘要
采用羟自由基氧化体系(H2O2浓度为0、0. 5、1、5和10 mmol/L)对猪肉肌原纤维蛋白进行不同氧化程度处理,研究氧化对蛋白质理化特性和凝胶水分分布的影响。结果表明,随H2O2浓度升高,猪肉肌原纤维蛋白游离巯基含量下降,表面疏水性增加,二聚酪氨酸含量升高,内源色氨酸荧光强度降低,说明蛋白质氧化程度增加。随H2O2浓度升高,蛋白凝胶的蒸煮得率、白度和保水性均显著下降(P <0. 05),与对照组相比,10 mmol/L组分别下降了22. 4%、4. 33%和16. 47%。低场核磁共振结果显示,氧化处理不影响凝胶的结合水含量,但会显著影响不易流动水和自由水的比例。随H2O2浓度升高,凝胶中的不易流动水含量降低,自由水增加,与凝胶保水性结果一致。相关性分析表明,凝胶保水性与蛋白质侧链氧化程度密切相关。
The effects of 0,0. 5,1,5 and 10 mmol/L H2 O2 induced oxidation on gelling water distribution and physicochemical properties of pork myofibrillar protein( MP) gels were investigated. The results showed that in MP,free sulfydryl content declined and surface hydrophobicity steadily increased with increasing H2 O2 concentration. Moreover,the content of dityrosine increased slightly,and the fluorescence intensity of tryptophan gradually decreased,which indicated that the oxidation level of protein increased. Additionally,the boiling rate,whiteness,and water holding capacity of gels decreased significantly( P < 0. 05). Compared with the control,the boiling rate,whiteness,and water holding capacity of gels declined by 22. 4%,4. 33%,and 16. 47%,respectively,by 10 mmol/L H2 O2.The low-field NMR showed that the oxidation degree of protein had no effects on bound water level in gels,but had significant effects on the ratio of immobile water to free water. Levels of immobile water and free water declined and increased,respectively,with increasing H2 O2 concentration,which was consistent with the water holding capacity of gels. It was also found that the water holding capacity of gels was closely correlated with the oxidation degree of protein side chains.
The effects of 0,0. 5,1,5 and 10 mmol/L H2 O2 induced oxidation on gelling water distribution and physicochemical properties of pork myofibrillar protein( MP) gels were investigated. The results showed that in MP,free sulfydryl content declined and surface hydrophobicity steadily increased with increasing H2 O2 concentration. Moreover,the content of dityrosine increased slightly,and the fluorescence intensity of tryptophan gradually decreased,which indicated that the oxidation level of protein increased. Additionally,the boiling rate,whiteness,and water holding capacity of gels decreased significantly( P < 0. 05). Compared with the control,the boiling rate,whiteness,and water holding capacity of gels declined by 22. 4%,4. 33%,and 16. 47%,respectively,by 10 mmol/L H2 O2.The low-field NMR showed that the oxidation degree of protein had no effects on bound water level in gels,but had significant effects on the ratio of immobile water to free water. Levels of immobile water and free water declined and increased,respectively,with increasing H2 O2 concentration,which was consistent with the water holding capacity of gels. It was also found that the water holding capacity of gels was closely correlated with the oxidation degree of protein side chains.
引文
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[15]胡忠良,邹玉峰,林玉海,等.氧化程度对肌原纤维蛋白热凝胶及理化特性的影响[J].食品科学,2013,34(17):19-23.
[16]陈霞霞,杨文鸽,吕梁玉,等.羟自由基氧化体系对银鲳肌原纤维蛋白生化特性及其构象单元的影响[J].食品科学,2016,37(23):123-128.
[17]李玲,季慧,段家玉.绿原酸抑制猪肉肌原纤维蛋白氧化及NDEA生成的作用研究[J].食品工业科技,2018,39(8):29-33.
[18] SUN W,ZHOU F,SUN D W,et al. Effect of oxidation on the emulsifying properties of myofibrillar proteins[J]. Food&Bioprocess Technology,2013,6(7):1 703-1 712.
[19] XIONG Y L,PARK D,OOIZUMI T. Variation in the cross-linking pattern of porcine myofibrillar protein exposed to three oxidative environments[J]. Journal of Agricultural&Food Chemistry,2009,57(1):153-159.
[20] ZHANG T,XUE Y,LI Z,et al. Effects of ozone-induced oxidation on the physicochemical properties of myofibrillar proteins recovered from bighead carp(Hypophthalmichthys nobilis)[J]. Food&Bioprocess Technology,2015,8(1):181-190.
[21] XIA X,KONG B,XIONG Y,et al. Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation[J]. Meat Science,2010,85(3):481-486.
[22] PEARCE K L,ROSENVOLD K,ANDERSEN H J,et al. Water distribution and mobility in meat during the conversion of muscle to meat and ageing and the impacts on fresh meat quality attributes—A review[J]. Meat Science,2011,89(2):111-124.
[23] SHAO J H,DENG Y M,JIA N,et al. Low-field NMR determination of water distribution in meat batters with Na Cl and polyphosphate addition[J]. Food Chemistry,2016,200:308-314.
[24] WANG L,ZHANG M,BHANDARI B,et al. Effects of malondialdehyde-induced protein modification on water functionality and physicochemical state of fish myofibrillar protein gel[J]. Food Research International,2016,86:131-139.
[25] LI C,LIU D,ZHOU G,et al. Meat quality and cooking attributes of thawed pork with different low field NMR T21[J]. Meat Science,2012,92(2):79-83.
[26] BERTRAM H C,ANDERSEN H J,KARLSSON A H.Comparative study of low-field NMR relaxation measurements and two traditional methods in the determination of water holding capacity of pork[J]. Meat Science,2001,57(2):125-132.
[2] 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,2007,101(3):1 239-1 246.
[3]李银,李侠,张春晖,等.羟自由基导致肉类肌原纤维蛋白氧化和凝胶性降低[J].农业工程学报,2013(12):286-292.
[4] CAO Y,XIONG Y L. Chlorogenic acid-mediated gel formation of oxidatively stressed myofibrillar protein[J]. Food Chemistry,2015,180:235-243
[5] FENG X,CHEN L,LEI N,et al. Emulsifying properties of oxidatively stressed myofibrillar protein emulsion Gels prepared with(-)-epigallocatechin-3-gallate and Na Cl[J]. Journal of Agricultural and Food Chemistry,2017,65(13):2 816-2 826.
[6] HAN M,WANG P,XU X,et al. Low-field NMR study of heat-induced gelation of pork myofibrillar proteins and its relationship with microstructural characteristics[J]. Food Research International,2014,62:1 175-1 182.
[7] NIU H,CHEN Y,ZHANG H,et al. Protective effect of porcine plasma protein hydrolysates on the gelation of porcine myofibrillar protein exposed to a hydroxyl radical-generating system[J]. International Journal of Biological Macromolecules,2018,107:654-661.
[8] ZHUANG X,JIANG X,HAN M,et al. Influence of sugarcane dietary fiber on water states and microstructure of myofibrillar protein gels[J]. Food Hydrocolloids,2016,57:253-261.
[9]梁慧,于立梅,陈秀兰,等.多酚对鸡肉氧化脂肪诱导蛋白质变性的影响[J].食品与发酵工业,2016,42(5):146-151.
[10] 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,2007,101(3):1 239-1 246.
[11] XIONG Y L,BLANCHARD S P,OOIZUMI T,et al.Hydroxyl radical and ferryl-generating systems promote gel network formation of myofibrillar protein[J]. Journal of Food Science,2010,75(2):C215-C221.
[12] XIA X,KONG B,LIU Q,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.
[13]李学鹏,周凯,周明言,等.自由基氧化对大黄鱼肌原纤维蛋白交联和聚集的影响[J].中国食品学报,2015,15(4):13-21.
[14] JI H,DONG S,HAN F,et al. Effects of dielectric barrier discharge(DBD)cold plasma treatment on physicochemical and functional properties of peanut protein[J].Food&Bioprocess Technology,2018,11(2):344-354.
[15]胡忠良,邹玉峰,林玉海,等.氧化程度对肌原纤维蛋白热凝胶及理化特性的影响[J].食品科学,2013,34(17):19-23.
[16]陈霞霞,杨文鸽,吕梁玉,等.羟自由基氧化体系对银鲳肌原纤维蛋白生化特性及其构象单元的影响[J].食品科学,2016,37(23):123-128.
[17]李玲,季慧,段家玉.绿原酸抑制猪肉肌原纤维蛋白氧化及NDEA生成的作用研究[J].食品工业科技,2018,39(8):29-33.
[18] SUN W,ZHOU F,SUN D W,et al. Effect of oxidation on the emulsifying properties of myofibrillar proteins[J]. Food&Bioprocess Technology,2013,6(7):1 703-1 712.
[19] XIONG Y L,PARK D,OOIZUMI T. Variation in the cross-linking pattern of porcine myofibrillar protein exposed to three oxidative environments[J]. Journal of Agricultural&Food Chemistry,2009,57(1):153-159.
[20] ZHANG T,XUE Y,LI Z,et al. Effects of ozone-induced oxidation on the physicochemical properties of myofibrillar proteins recovered from bighead carp(Hypophthalmichthys nobilis)[J]. Food&Bioprocess Technology,2015,8(1):181-190.
[21] XIA X,KONG B,XIONG Y,et al. Decreased gelling and emulsifying properties of myofibrillar protein from repeatedly frozen-thawed porcine longissimus muscle are due to protein denaturation and susceptibility to aggregation[J]. Meat Science,2010,85(3):481-486.
[22] PEARCE K L,ROSENVOLD K,ANDERSEN H J,et al. Water distribution and mobility in meat during the conversion of muscle to meat and ageing and the impacts on fresh meat quality attributes—A review[J]. Meat Science,2011,89(2):111-124.
[23] SHAO J H,DENG Y M,JIA N,et al. Low-field NMR determination of water distribution in meat batters with Na Cl and polyphosphate addition[J]. Food Chemistry,2016,200:308-314.
[24] WANG L,ZHANG M,BHANDARI B,et al. Effects of malondialdehyde-induced protein modification on water functionality and physicochemical state of fish myofibrillar protein gel[J]. Food Research International,2016,86:131-139.
[25] LI C,LIU D,ZHOU G,et al. Meat quality and cooking attributes of thawed pork with different low field NMR T21[J]. Meat Science,2012,92(2):79-83.
[26] BERTRAM H C,ANDERSEN H J,KARLSSON A H.Comparative study of low-field NMR relaxation measurements and two traditional methods in the determination of water holding capacity of pork[J]. Meat Science,2001,57(2):125-132.
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