三聚磷酸钠对猪肉肌原纤维蛋白功能特性的影响
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摘要
以猪肉肌原纤维蛋白(myofibril protein,MP)为研究对象,探讨不同质量浓度三聚磷酸钠(sodiumtripolyphosphate,STP)的添加对MP乳化性、乳化稳定性、起泡性等7个功能特性指标的影响,并进行相关性分析。结果表明:随着STP质量浓度升高,MP的乳化性、乳化稳定性、起泡性、起泡稳定性、凝胶强度和凝胶保水性均呈上升趋势,表面疏水性呈下降趋势;MP的起泡性和凝胶强度在STP质量浓度为0.3 g/100 mL时最大,乳化性、表面疏水性和凝胶保水性在STP质量浓度为0.4 g/100 mL时效果最佳;MP的起泡性、起泡稳定性和乳化性呈极显著正相关(P<0.01),乳化性与乳化稳定性呈显著正相关(P<0.05),乳化性、乳化稳定性、起泡性、起泡稳定性与表面疏水性呈极显著负相关(P<0.01),与凝胶保水性呈极显著正相关(P<0.01),表面疏水性与凝胶保水性呈极显著负相关(P<0.01),表面疏水性与凝胶强度呈极显著正相关(P<0.01)。STP可以增强MP的功能特性,其质量浓度为0.3~0.4 g/100 mL时效果最佳。改善乳化性、起泡性和表面疏水性等界面性质可以增强MP的凝胶特性。
The objective of this study was to evaluate the effect of different concentrations of sodium tripolyphosphate(STP) on 7 functional characteristics of pork myofibrillar protein(MP) such as emulsifying capacity, emulsion stability and foaming characteristics, and correlation analysis was performed. The results showed that emulsifying capacity,emulsion stability, foaming property, foam stability, gel strength and water-retaining property were increased while surface hydrophobicity was decreased with increasing concentration of STP. The maximum foaming capacity and gel strength were obtained at a STP concentration of 0.3 g/100 mL, whereas the best emulsifying capacity, surface hydrophobicity, gel strength and water-retaining property were obtained at 0.4 g/100 mL. There was a significant positive correlation between foaming capacity and foam stability and emulsifying capacity(P < 0.01), and emulsifying capacity was significantly positively correlated with emulsion stability(P < 0.05). Emulsifying capacity, emulsion stability and foam stability were significantly positively correlated with surface hydrophobicity(P < 0.01) and negatively correlated with gel water-retaining property(P < 0.01). In conclusion, sodium tripolyphosphate could enhance the functional properties of myofibrillar protein and the optimum concentration was 0.3-0.4 g/100 mL. Improving the interfacial properties emulsifying capacity, foaming characteristics and surface hydrophobicity could enhance the gel properties of myofibrillar proteins
The objective of this study was to evaluate the effect of different concentrations of sodium tripolyphosphate(STP) on 7 functional characteristics of pork myofibrillar protein(MP) such as emulsifying capacity, emulsion stability and foaming characteristics, and correlation analysis was performed. The results showed that emulsifying capacity,emulsion stability, foaming property, foam stability, gel strength and water-retaining property were increased while surface hydrophobicity was decreased with increasing concentration of STP. The maximum foaming capacity and gel strength were obtained at a STP concentration of 0.3 g/100 mL, whereas the best emulsifying capacity, surface hydrophobicity, gel strength and water-retaining property were obtained at 0.4 g/100 mL. There was a significant positive correlation between foaming capacity and foam stability and emulsifying capacity(P < 0.01), and emulsifying capacity was significantly positively correlated with emulsion stability(P < 0.05). Emulsifying capacity, emulsion stability and foam stability were significantly positively correlated with surface hydrophobicity(P < 0.01) and negatively correlated with gel water-retaining property(P < 0.01). In conclusion, sodium tripolyphosphate could enhance the functional properties of myofibrillar protein and the optimum concentration was 0.3-0.4 g/100 mL. Improving the interfacial properties emulsifying capacity, foaming characteristics and surface hydrophobicity could enhance the gel properties of myofibrillar proteins
引文
[1] ASGHAR A, SAMEJIMA K, YASUI T. Functionality of muscle proteins in gelation mechanisms of structured meat products[J].C R C Critical Reviews in Food Technology, 1985, 22(1):27-106.DOI:10.1080/10408398509527408.
[2] LANIER T C, CARVAJAL P, YONGSAWATDIGUL J, et al. Surimi gelation chemistry[M]. Oxford:Elsevier, 2005:425-489.
[3]孔保华,王宇,夏秀芳,等.加热温度对猪肉肌原纤维蛋白凝胶特性的影响[J].食品科学,2011,32(5):50-54. DOI:10.7506/spkx1002-6630-201105011.
[4] BAUBLITS R T, POHLMAN F W, BROWN A H, Jr, et al. Effects of enhancement with varying phosphate types and concentrations, at two different pump rates on beef biceps femoris instrumental color characteristics[J]. Meat Science, 2005, 71(2):264-276. DOI:10.1016/j. meatsci.2005.03.015.
[5]段昌圣,赵双娟,黄文,等.三聚磷酸盐对鸭肉品质的影响[J].食品科学,2013, 34(7):62-66. DOI:10.7506/spkx1002-6630-201307014.
[6] WESTPHALEN A D, BRIGGS J L, LONERGAN S M. Influence of pH rheological properties of porcine myofibrillar protein during heat induced gelation[J]. Meat Science, 2005, 70:293-299. DOI:10.1016/j.meatsci.2005.01.015.
[7] FUKAZAWA T, HASHIMOTO Y, YASUI T. The relationship between the components of myofibrillar protein and their effect ofvarious phosphates that influence the binding quality of sausage[J].Food Science, 1961, 26(5):550-555. DOI:10.1111/j.1365-2621.1961.tb00404.x.
[8] EILERT S J, MANDIGO R W, SUMNER S S. Phosphate and modified beef connective tissue effects on reduced fat, high wateradded frankfurters[J]. Journal of Food Science, 1996, 61(5):1006-1012. DOI:10.1111/j. 1365-2621.1996.tb10921.x.
[9] XIONG YoulingL. A comparison of the rheological characteristics of different fraction of chicken myofibrillar proteins[J]. Journal of Food Biochemistry, 1993. 16(4):217-227. DOI:10.1111/j.1745-4514.1992.tb00447.x.
[10] AGYARE K K, ADDO K, XIONG Y L. Emulsifying and foaming properties of transglutaminase-treated wheat gluten hydrolysate as influenced by pH, temperature and salt[J]. Food Hydrocolloids, 2009,23(1):72-81. DOI:10.1016/j.foodhyd.2007.11.012.
[11] WANG Guang, WANG Tong. Effects of yolk contamination, shearing,and heating on foaming properties of fresh egg white[J]. Journal of Food Science,2010, 74(2):C147-C156. DOI:10.1111/j.1750-3841.2009.01054.x.
[12] CHELH I,GATELLIER P,SANTE-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.
[13]赵冰,李素,张顺亮,等.蛋白氧化对肌原纤维蛋白凝胶构效关系的影响[J].食品科学,2018, 39(3):55-61. DOI:10.7506/spkx1002-6630-201803009.
[14]赵冰,李家鹏,陈文华,等.可得然胶凝胶特性及其在西式火腿中的应用研究[J].食品科学,2014, 35(21):45-49. DOI:10.7506/spkx1002-6630-201421010.
[15]常辰曦,邹玉峰,曹锦轩,等.谷氨酸螯合钙替代部分食盐对兔肉肌原纤维蛋白热凝胶和乳化特性的影响[J].食品科学,2014, 35(7):1-6. DOI:10.7506/spkx 1002-6630-201407001.
[16] ZORBA O, GOKALP H Y, YETIM H, et al. Model system evaluations of the effects of different levels of K2HPO4, NaCl and oil temperature on emulsion stability and viscosity of fresh and frozen turkish style meat emulsions[J]. Meat Science, 1993, 34(2):145-161.DOI:10.1016/0309-1740(93)90024-C.
[17] DICKINSON E. Structure formation in casein-based gels, foams,and emulsions[J]. Colloids and Surfaces A:Physicochemical and Engineering Aspects, 2006, 288(1/3):3-11. DOI:10.1016/j.colsurfa.2006.01.012.
[18] YAPAR A, ATAY S, KAYACIER A, et al. Effects of different levels of salt and phosphate on some emulsion attributes of the common carp(Cyprinus carpio L. 1758)[J]. Food Hydrocolloids, 2006, 20(6):825-830. DOI:10.1016/j.foodhyd.2005.08.005.
[19] SANCHEZ C C, PATINO J M R. Interfacial, foaming and emulsifying characteristics of sodium caseinate as influenced by protein concentration in solution[J]. Food Hydrocolloids, 2005, 19(3):407-416. DOI:10.1016/j.foodhyd.2004.10.007.
[20]荣婧,仇超颖,胡晓,等.鸢乌贼肌原纤维蛋白糖基化产物功能特性研究[J].南方水产科学,2018, 14(1):68-76. DOI:10.3969/j.issn.2095-0780.2018.01.009.
[21] O'DONNELL C P,TIWARI B K,BOURKE P,et al. Effect of ultrasonic processing on food enzymes of industrial importance[J].Trends in Food Science and Technology, 2010, 21(7):358-367.DOI:10.1016/j.tifs.2010.04.007.
[22]李瑜,尹春明,周瑞宝.三聚磷酸钠改性小麦面筋蛋白研究[J].粮食与油脂,2002(2):4-5. DOI:10.3969/j.issn.1008-9578.2002.02.002.
[23] RIEBROY S, BENJAKUL S, VISESSANGUAN W, et al. Acidinduced gelation of natural actomyosin from Atlantic cod(Gadus morhua)and burbot(Lota lota)[J]. Food Hydrocolloids, 2009, 23(1):26-39. DOI:10.1016/j.foodhyd.2007.11.010.
[24] DAVILA E, PARES D, CUVELIER G, et al. Heat-induced gelation of porcine blood plasma proteins as affected by pH[J]. Meat Science,2007, 76:216-225. DOI:10.1016/j.meatsci.2006.11.002.
[25]邓丽,芮汉明.Ca2+、Mg2+和磷酸盐对鸡肉盐溶蛋白质凝胶保水性和凝胶特性影响的研究[J].现代食品科技,2005, 21(2):24-26.DOI:10.3969/j.issn. 1673-9078.2005.02.008.
[26] SAGUER E, ALVAREZ P A, SEDMAN J, et al. Study of the denaturation/aggregation behavior of whole porcine plasma and its protein fractions during heating under acidic pH by variabletemperature FTIR spectroscopy[J]. Food Hydrocolloids, 2013, 33(2):402-414. DOI:10.1016/j.foodhyd.2013.04.017.
[27] XIONG YoulingL. Role of myofibrillar proteins in water-binding in brine-enhance dmeats[J]. Food Research International, 2005, 38(3):281-287. DOI:10.1016/j.foodres.2004.03.013.
[28] HAMM R. Muscle As Food:4-Functional properties of the myofibrillar system and their measurements[J]. Salt Lake City:Academic Press, 1986:135-199. DOI:10.1016/B978-0-12-084190-5.50009-6.
[29] LI Chunqiang, XIONG YoulingL, CHEN Jie. Oxidation-induced unfolding facilitates myosin cross-linking in myofibrillar protein by microbial transglutaminase[J]. Journal of Agricultural and Food Chemistry, 2012, 60(32):8020-8027. DOI:10.1021/jf302150h.
[30]徐幸莲,王霞,周光宏,等.磷酸盐对肌球蛋白热凝胶硬度、保水性和超微结构的影响[J].食品科学,2005, 26(3):42-46. DOI:10.3321/j.issn:1002-6630.2005.03.004.
[31] RODRIGUEZ M R, RODRIGUEZD NINO M R, WILDE P J, et al.Rheokinetic analysis of protein films at the air-aqueous subphase interface. 2. Bovine serum albumin adsorption from sucrose aqueous solutions[J]. Journal of Agricultural and Food Chemistry, 1997, 45(8):3010-3015.
[32]阚健全,陈宗道,杨辉,等.蛋白质溶液表面张力及其与功能性质的关系[J].中国粮油学报,1999(5):30-34. DOI:10.1017/S0266078400010713.
[33] GRAHAM D E, PHILLIPS M C. Proteins at liquid interfaces:I.Kinetics of adsorption and surface denaturation[J]. Journal of Colloid and Interface Science, 1979, 70(3):403-414. DOI:10.1016/0021-9797(79)90048-1.
[34] NAKAI S. Structure-function relationships of food proteins:with an emphasis on the importance of protein hydrophobicity[J]. Journal of Agricultural and Food Chemistry, 1983, 31(4):676-683. DOI:10.1021/jf00118a001.
[35]郑文彬,韩晶,王颖,等.黑龙江省芸豆主栽品种蛋白质功能性质分析[J].中国粮油学报,2017, 32(2):6-12. DOI:10.3969/j.issn.1003-0174.2017.02.002.
[36]周心雅,贺稚非,李洪军,等.酸碱度对兔肉肌原纤维蛋白功能性质的影响[J].食品与发酵工业,2017(11):176-183. DOI:10.13995/j.cnki.11-1802/ts.014272.
[37]王静宇,杨玉玲,康大成,等.超声波对肌原纤维蛋白热诱导凝胶化学作用力与保水性的影响[J].中国农业科学,2017, 50(12):2349-2358. DOI:10.3864/j.issn.0578-1752.2017.12.015.
[2] LANIER T C, CARVAJAL P, YONGSAWATDIGUL J, et al. Surimi gelation chemistry[M]. Oxford:Elsevier, 2005:425-489.
[3]孔保华,王宇,夏秀芳,等.加热温度对猪肉肌原纤维蛋白凝胶特性的影响[J].食品科学,2011,32(5):50-54. DOI:10.7506/spkx1002-6630-201105011.
[4] BAUBLITS R T, POHLMAN F W, BROWN A H, Jr, et al. Effects of enhancement with varying phosphate types and concentrations, at two different pump rates on beef biceps femoris instrumental color characteristics[J]. Meat Science, 2005, 71(2):264-276. DOI:10.1016/j. meatsci.2005.03.015.
[5]段昌圣,赵双娟,黄文,等.三聚磷酸盐对鸭肉品质的影响[J].食品科学,2013, 34(7):62-66. DOI:10.7506/spkx1002-6630-201307014.
[6] WESTPHALEN A D, BRIGGS J L, LONERGAN S M. Influence of pH rheological properties of porcine myofibrillar protein during heat induced gelation[J]. Meat Science, 2005, 70:293-299. DOI:10.1016/j.meatsci.2005.01.015.
[7] FUKAZAWA T, HASHIMOTO Y, YASUI T. The relationship between the components of myofibrillar protein and their effect ofvarious phosphates that influence the binding quality of sausage[J].Food Science, 1961, 26(5):550-555. DOI:10.1111/j.1365-2621.1961.tb00404.x.
[8] EILERT S J, MANDIGO R W, SUMNER S S. Phosphate and modified beef connective tissue effects on reduced fat, high wateradded frankfurters[J]. Journal of Food Science, 1996, 61(5):1006-1012. DOI:10.1111/j. 1365-2621.1996.tb10921.x.
[9] XIONG YoulingL. A comparison of the rheological characteristics of different fraction of chicken myofibrillar proteins[J]. Journal of Food Biochemistry, 1993. 16(4):217-227. DOI:10.1111/j.1745-4514.1992.tb00447.x.
[10] AGYARE K K, ADDO K, XIONG Y L. Emulsifying and foaming properties of transglutaminase-treated wheat gluten hydrolysate as influenced by pH, temperature and salt[J]. Food Hydrocolloids, 2009,23(1):72-81. DOI:10.1016/j.foodhyd.2007.11.012.
[11] WANG Guang, WANG Tong. Effects of yolk contamination, shearing,and heating on foaming properties of fresh egg white[J]. Journal of Food Science,2010, 74(2):C147-C156. DOI:10.1111/j.1750-3841.2009.01054.x.
[12] CHELH I,GATELLIER P,SANTE-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.
[13]赵冰,李素,张顺亮,等.蛋白氧化对肌原纤维蛋白凝胶构效关系的影响[J].食品科学,2018, 39(3):55-61. DOI:10.7506/spkx1002-6630-201803009.
[14]赵冰,李家鹏,陈文华,等.可得然胶凝胶特性及其在西式火腿中的应用研究[J].食品科学,2014, 35(21):45-49. DOI:10.7506/spkx1002-6630-201421010.
[15]常辰曦,邹玉峰,曹锦轩,等.谷氨酸螯合钙替代部分食盐对兔肉肌原纤维蛋白热凝胶和乳化特性的影响[J].食品科学,2014, 35(7):1-6. DOI:10.7506/spkx 1002-6630-201407001.
[16] ZORBA O, GOKALP H Y, YETIM H, et al. Model system evaluations of the effects of different levels of K2HPO4, NaCl and oil temperature on emulsion stability and viscosity of fresh and frozen turkish style meat emulsions[J]. Meat Science, 1993, 34(2):145-161.DOI:10.1016/0309-1740(93)90024-C.
[17] DICKINSON E. Structure formation in casein-based gels, foams,and emulsions[J]. Colloids and Surfaces A:Physicochemical and Engineering Aspects, 2006, 288(1/3):3-11. DOI:10.1016/j.colsurfa.2006.01.012.
[18] YAPAR A, ATAY S, KAYACIER A, et al. Effects of different levels of salt and phosphate on some emulsion attributes of the common carp(Cyprinus carpio L. 1758)[J]. Food Hydrocolloids, 2006, 20(6):825-830. DOI:10.1016/j.foodhyd.2005.08.005.
[19] SANCHEZ C C, PATINO J M R. Interfacial, foaming and emulsifying characteristics of sodium caseinate as influenced by protein concentration in solution[J]. Food Hydrocolloids, 2005, 19(3):407-416. DOI:10.1016/j.foodhyd.2004.10.007.
[20]荣婧,仇超颖,胡晓,等.鸢乌贼肌原纤维蛋白糖基化产物功能特性研究[J].南方水产科学,2018, 14(1):68-76. DOI:10.3969/j.issn.2095-0780.2018.01.009.
[21] O'DONNELL C P,TIWARI B K,BOURKE P,et al. Effect of ultrasonic processing on food enzymes of industrial importance[J].Trends in Food Science and Technology, 2010, 21(7):358-367.DOI:10.1016/j.tifs.2010.04.007.
[22]李瑜,尹春明,周瑞宝.三聚磷酸钠改性小麦面筋蛋白研究[J].粮食与油脂,2002(2):4-5. DOI:10.3969/j.issn.1008-9578.2002.02.002.
[23] RIEBROY S, BENJAKUL S, VISESSANGUAN W, et al. Acidinduced gelation of natural actomyosin from Atlantic cod(Gadus morhua)and burbot(Lota lota)[J]. Food Hydrocolloids, 2009, 23(1):26-39. DOI:10.1016/j.foodhyd.2007.11.010.
[24] DAVILA E, PARES D, CUVELIER G, et al. Heat-induced gelation of porcine blood plasma proteins as affected by pH[J]. Meat Science,2007, 76:216-225. DOI:10.1016/j.meatsci.2006.11.002.
[25]邓丽,芮汉明.Ca2+、Mg2+和磷酸盐对鸡肉盐溶蛋白质凝胶保水性和凝胶特性影响的研究[J].现代食品科技,2005, 21(2):24-26.DOI:10.3969/j.issn. 1673-9078.2005.02.008.
[26] SAGUER E, ALVAREZ P A, SEDMAN J, et al. Study of the denaturation/aggregation behavior of whole porcine plasma and its protein fractions during heating under acidic pH by variabletemperature FTIR spectroscopy[J]. Food Hydrocolloids, 2013, 33(2):402-414. DOI:10.1016/j.foodhyd.2013.04.017.
[27] XIONG YoulingL. Role of myofibrillar proteins in water-binding in brine-enhance dmeats[J]. Food Research International, 2005, 38(3):281-287. DOI:10.1016/j.foodres.2004.03.013.
[28] HAMM R. Muscle As Food:4-Functional properties of the myofibrillar system and their measurements[J]. Salt Lake City:Academic Press, 1986:135-199. DOI:10.1016/B978-0-12-084190-5.50009-6.
[29] LI Chunqiang, XIONG YoulingL, CHEN Jie. Oxidation-induced unfolding facilitates myosin cross-linking in myofibrillar protein by microbial transglutaminase[J]. Journal of Agricultural and Food Chemistry, 2012, 60(32):8020-8027. DOI:10.1021/jf302150h.
[30]徐幸莲,王霞,周光宏,等.磷酸盐对肌球蛋白热凝胶硬度、保水性和超微结构的影响[J].食品科学,2005, 26(3):42-46. DOI:10.3321/j.issn:1002-6630.2005.03.004.
[31] RODRIGUEZ M R, RODRIGUEZD NINO M R, WILDE P J, et al.Rheokinetic analysis of protein films at the air-aqueous subphase interface. 2. Bovine serum albumin adsorption from sucrose aqueous solutions[J]. Journal of Agricultural and Food Chemistry, 1997, 45(8):3010-3015.
[32]阚健全,陈宗道,杨辉,等.蛋白质溶液表面张力及其与功能性质的关系[J].中国粮油学报,1999(5):30-34. DOI:10.1017/S0266078400010713.
[33] GRAHAM D E, PHILLIPS M C. Proteins at liquid interfaces:I.Kinetics of adsorption and surface denaturation[J]. Journal of Colloid and Interface Science, 1979, 70(3):403-414. DOI:10.1016/0021-9797(79)90048-1.
[34] NAKAI S. Structure-function relationships of food proteins:with an emphasis on the importance of protein hydrophobicity[J]. Journal of Agricultural and Food Chemistry, 1983, 31(4):676-683. DOI:10.1021/jf00118a001.
[35]郑文彬,韩晶,王颖,等.黑龙江省芸豆主栽品种蛋白质功能性质分析[J].中国粮油学报,2017, 32(2):6-12. DOI:10.3969/j.issn.1003-0174.2017.02.002.
[36]周心雅,贺稚非,李洪军,等.酸碱度对兔肉肌原纤维蛋白功能性质的影响[J].食品与发酵工业,2017(11):176-183. DOI:10.13995/j.cnki.11-1802/ts.014272.
[37]王静宇,杨玉玲,康大成,等.超声波对肌原纤维蛋白热诱导凝胶化学作用力与保水性的影响[J].中国农业科学,2017, 50(12):2349-2358. DOI:10.3864/j.issn.0578-1752.2017.12.015.