常见热杀菌方式对关中羊乳品质的影响
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摘要
采用5种常用热杀菌方式处理关中羊乳,即低温长时巴氏杀菌(65℃/30 min)、高温短时巴氏杀菌(72℃/15 s)、超巴氏杀菌(95℃/5 min)、高温高压灭菌(121℃/20 min)和超高温瞬时灭菌(137℃/7 s),在测定蛋白沉淀率、酒精稳定性、pH、红度值、粘度和脂肪球变化基础上,结合内源荧光光谱和聚丙烯酰胺凝胶电泳(SDS-PAGE)分析,探究热杀菌处理对关中羊乳品质的影响。结果表明,高温高压灭菌羊乳蛋白沉淀率最高、酒精稳定性最差、pH明显下降、红度值明显增大,但5种杀菌方式对粘度没有显著影响(p>0.05);羊乳脂肪球经巴氏杀菌和超巴氏杀菌后,表观直径略微增大,而高温高压灭菌和超高温瞬时灭菌,尤其是高温高压灭菌则导致其明显变小;荧光光谱表明,高温高压灭菌羊乳蛋白结构改变最大,内源荧光强度剧烈升高;电泳显示,巴氏杀菌(65℃/30 min和72℃/15 s)对羊乳酪蛋白和乳清蛋白影响较小,超巴氏杀菌(95℃/5 min)乳清蛋白开始变性、聚集或部分降解,高温高压灭菌和超高温瞬时灭菌,尤其是高温高压灭菌则使乳清蛋白明显降解甚至消失,酪蛋白出现聚集和解聚。结果表明,高温高压灭菌和超高温瞬时灭菌,尤其是高温高压灭菌对关中羊乳品质影响较大,超巴氏杀菌影响次之,而巴氏杀菌则对其影响较小。
Guanzhong goat milk was treated by five common thermal sterilization:low temperature long-time pasteurization(65 ℃/30 min),high temperature short-time pasteurization(72 ℃/15 s),ultra-pasteurization(95 ℃/5 min),high temperature high pressure sterilization(121 ℃/20 min)and ultra-high temperature instantaneous sterilization(137 ℃/7 s)in this research,and protein precipitation rate,alcohol stability,pH,color value,viscosity and fat ball,as well as endogenous fluorescence spectrum and SDS-PAGE were measured to explore the influence of thermal sterilization on quality of goat milk. The results showed that goat milk treated by high temperature high pressure sterilization displayed the highest protein precipitation rate,the lowest alcohol stability,significant pH reduction and red value increase,while viscosity showed no significant difference among five thermal sterilization methods. Moreover,fat ball diameter increased slightly for pasteurization and ultra-pasteurization versus obvious decrease for high temperature high pressure sterilization and ultra-high temperature instantaneous sterilization especially high temperature high pressure sterilization. In addition,high temperature high pressure sterilization resulted in dramatically increase of endogenous fluorescence intensity,which indicated obvious change of milk protein structure. SDS-PAGE showed 65 ℃/30 min and 72 ℃/15 s pasteurization had limited effect on casein and whey protein;95 ℃/5 min ultra-pasteurization caused whey protein to denature,aggregate and slightly degrade;137 ℃/7 s especially 121 ℃/20 min,brought obvious dissociation or even disappearance for whey protein,and polymerization as well as depolymerization for casein. Therefore,ultra-high temperature especially high-pressure sterilization had more obvious impact on the quality of Guanzhong Goat milk,followed by ultra-pasteurization,while pasteurization had small impact.
Guanzhong goat milk was treated by five common thermal sterilization:low temperature long-time pasteurization(65 ℃/30 min),high temperature short-time pasteurization(72 ℃/15 s),ultra-pasteurization(95 ℃/5 min),high temperature high pressure sterilization(121 ℃/20 min)and ultra-high temperature instantaneous sterilization(137 ℃/7 s)in this research,and protein precipitation rate,alcohol stability,pH,color value,viscosity and fat ball,as well as endogenous fluorescence spectrum and SDS-PAGE were measured to explore the influence of thermal sterilization on quality of goat milk. The results showed that goat milk treated by high temperature high pressure sterilization displayed the highest protein precipitation rate,the lowest alcohol stability,significant pH reduction and red value increase,while viscosity showed no significant difference among five thermal sterilization methods. Moreover,fat ball diameter increased slightly for pasteurization and ultra-pasteurization versus obvious decrease for high temperature high pressure sterilization and ultra-high temperature instantaneous sterilization especially high temperature high pressure sterilization. In addition,high temperature high pressure sterilization resulted in dramatically increase of endogenous fluorescence intensity,which indicated obvious change of milk protein structure. SDS-PAGE showed 65 ℃/30 min and 72 ℃/15 s pasteurization had limited effect on casein and whey protein;95 ℃/5 min ultra-pasteurization caused whey protein to denature,aggregate and slightly degrade;137 ℃/7 s especially 121 ℃/20 min,brought obvious dissociation or even disappearance for whey protein,and polymerization as well as depolymerization for casein. Therefore,ultra-high temperature especially high-pressure sterilization had more obvious impact on the quality of Guanzhong Goat milk,followed by ultra-pasteurization,while pasteurization had small impact.
引文
[1]张巍,戴鼎丞. 陕西羊乳企业新型营销模式的构建[J]. 中国市场,2016,35:22-23.
[2]Liu Y,Guo R. pH-dependent structures and properties of casein micelles[J]. Biophysical Chemistry,2008,136(2-3):67-73.
[3]Mortier L,Braekman A,Cartuyvels D,et al. Intrinsic indicators for monitoring heat damage of consumption milk[J]. Biotechnologie Agronomie Societe et Environnement,2000,4(4):221-225.
[4]李林强,王亮,田苏辉,等. 牛羊乳蛋白质粒度对其热处理沉淀率的影响[J]. 食品与生物技术学报,2017,36(9):1002-1007.
[5]张富新,魏怡. 羊奶酪蛋白热稳性的研究[J]. 食品工业科技,2011(10):114-116.
[6]赵丽丽. 羊乳热稳定性及凝胶特性的研究[D].北京:中国农业科学院,2014.
[7]Pesic M B,Barac M B,Stanojevic S P,et al. Heat-induced casein-whey protein interactions at natural pH of milk:A comparison between caprine and bovine milk[J]. Small Ruminant Research,2012,108(1-3):77-86.
[8]孙琦. 牛乳热加工特性及其盐类平衡的研究[D].北京:中国农业科学院,2012.
[9]李子超,徐明芳,向明霞,等. 巴氏杀菌与超高温灭菌牛乳酪蛋白结构差异性的研究[J]. 华南农业大学学报,2013,34(2):192-196.
[10]Chevallet M,Luche S,Rabilloud T. Silver staining of proteins in polyacrylamide gels[J]. Nature Protocols,2006,1:1852-1858.
[11]Raynal-Ljutovac K,Park Y W,Gaucheron F,et al. Heat stability and enzymatic modifications of goat and sheep milk[J]. Small Ruminant Research,2007,68(1-2):207-220.
[12]周强. 羊乳理化特性及其胶体稳定性研究[D].西安:陕西师范大学,2007.
[13]史永翠,李钰,娄新曼,等. 羊乳酪蛋白稳定性分析[J]. 乳业科学与技术,2014,37(1):31-34.
[14]Jenness R,Patton S. Physical properties of milk[J]. Dairy Chemistry,1976:230-250.
[15]宋慧敏. 热处理对牛乳风味及保藏品质的影响[D]. 哈尔滨:东北农业大学,2015.
[16]Raikos V,Kapolos J,Farmakis L,et al. The use of sedimentation field-flow fractionation in the size characterization of bovine milk fat globules as affected by heat treatment[J]. Food Research International,2009:425-432.
[17]周洁瑾,张列兵,梁建芬. 加热及贮藏对牛乳脂肪及蛋白聚集影响的研究[J]. 食品科技,2010,35(5):72-76.
[18]Ye A,Anema S G,Singh H. High-pressure-induced interactions between milk fat globule membrane proteins and skimmilk proteins in whole milk[J]. Journal of Dairy Science,2004,87(12):4013-4022.
[19]张勇,段旭昌,白艳红,等. 超高压处理对牛乳微观特性影响的研究[J]. 食品科技,2008(3):115-118.
[20]吴新.脉冲电场对牛乳蛋白功能性质和结构的影响[D]. 无锡:江南大学,2009.
[21]刘燕.酪蛋白胶束结构与功能特性的研究[D].扬州:扬州大学,2007.
[22]Montilla A,Baleones E,Olano A,et al. Influence of heat treatments on whey protein denaturation and rennetelotting properties of cow and goat milk[J]. Journal of Agricultural and Food Chemistry,1995,43:1908-1911.
[23]Allmere T,Andrén A,Bj?rck L. Interactions between different genetic variants of β-lactoglobulin and κ-casein during heating of skim milk[J]. Journal of Agricultural and Food Chemistry,1997,45(5):1564-1569.
[24]Henry G,Mollé D,Morgan F,et al. Heat induced covalent complex between casein micelles and β-lactoglobulin from goats milk:Identification of an involved disulfide bond[J]. Journal of Agriculture Food Chemistry,2002,50:185-191.
[2]Liu Y,Guo R. pH-dependent structures and properties of casein micelles[J]. Biophysical Chemistry,2008,136(2-3):67-73.
[3]Mortier L,Braekman A,Cartuyvels D,et al. Intrinsic indicators for monitoring heat damage of consumption milk[J]. Biotechnologie Agronomie Societe et Environnement,2000,4(4):221-225.
[4]李林强,王亮,田苏辉,等. 牛羊乳蛋白质粒度对其热处理沉淀率的影响[J]. 食品与生物技术学报,2017,36(9):1002-1007.
[5]张富新,魏怡. 羊奶酪蛋白热稳性的研究[J]. 食品工业科技,2011(10):114-116.
[6]赵丽丽. 羊乳热稳定性及凝胶特性的研究[D].北京:中国农业科学院,2014.
[7]Pesic M B,Barac M B,Stanojevic S P,et al. Heat-induced casein-whey protein interactions at natural pH of milk:A comparison between caprine and bovine milk[J]. Small Ruminant Research,2012,108(1-3):77-86.
[8]孙琦. 牛乳热加工特性及其盐类平衡的研究[D].北京:中国农业科学院,2012.
[9]李子超,徐明芳,向明霞,等. 巴氏杀菌与超高温灭菌牛乳酪蛋白结构差异性的研究[J]. 华南农业大学学报,2013,34(2):192-196.
[10]Chevallet M,Luche S,Rabilloud T. Silver staining of proteins in polyacrylamide gels[J]. Nature Protocols,2006,1:1852-1858.
[11]Raynal-Ljutovac K,Park Y W,Gaucheron F,et al. Heat stability and enzymatic modifications of goat and sheep milk[J]. Small Ruminant Research,2007,68(1-2):207-220.
[12]周强. 羊乳理化特性及其胶体稳定性研究[D].西安:陕西师范大学,2007.
[13]史永翠,李钰,娄新曼,等. 羊乳酪蛋白稳定性分析[J]. 乳业科学与技术,2014,37(1):31-34.
[14]Jenness R,Patton S. Physical properties of milk[J]. Dairy Chemistry,1976:230-250.
[15]宋慧敏. 热处理对牛乳风味及保藏品质的影响[D]. 哈尔滨:东北农业大学,2015.
[16]Raikos V,Kapolos J,Farmakis L,et al. The use of sedimentation field-flow fractionation in the size characterization of bovine milk fat globules as affected by heat treatment[J]. Food Research International,2009:425-432.
[17]周洁瑾,张列兵,梁建芬. 加热及贮藏对牛乳脂肪及蛋白聚集影响的研究[J]. 食品科技,2010,35(5):72-76.
[18]Ye A,Anema S G,Singh H. High-pressure-induced interactions between milk fat globule membrane proteins and skimmilk proteins in whole milk[J]. Journal of Dairy Science,2004,87(12):4013-4022.
[19]张勇,段旭昌,白艳红,等. 超高压处理对牛乳微观特性影响的研究[J]. 食品科技,2008(3):115-118.
[20]吴新.脉冲电场对牛乳蛋白功能性质和结构的影响[D]. 无锡:江南大学,2009.
[21]刘燕.酪蛋白胶束结构与功能特性的研究[D].扬州:扬州大学,2007.
[22]Montilla A,Baleones E,Olano A,et al. Influence of heat treatments on whey protein denaturation and rennetelotting properties of cow and goat milk[J]. Journal of Agricultural and Food Chemistry,1995,43:1908-1911.
[23]Allmere T,Andrén A,Bj?rck L. Interactions between different genetic variants of β-lactoglobulin and κ-casein during heating of skim milk[J]. Journal of Agricultural and Food Chemistry,1997,45(5):1564-1569.
[24]Henry G,Mollé D,Morgan F,et al. Heat induced covalent complex between casein micelles and β-lactoglobulin from goats milk:Identification of an involved disulfide bond[J]. Journal of Agriculture Food Chemistry,2002,50:185-191.