热处理对乳蛋白结构和消化特性的影响
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摘要
通过热处理对浓缩乳蛋白70(milk protein concentrate 70,MPC70)进行改性,研究改性对乳蛋白结构及消化性的影响。结果表明:乳蛋白经过25、75、85、95℃分别处理15min,随着热处理温度的增加,表面巯基含量和表面疏水性显著升高,在95℃时达到最高,分别为42μmol/L和1 008;经过热处理后,乳蛋白中α-螺旋和β-转角的含量下降,β-折叠和无规则卷曲含量上升;通过采用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析模拟胃肠消化样品发现,一定程度的热处理提升了乳蛋白的可消化性,这可能与其结构变化相关。
In this study, the effect of thermal modifications(25, 75, 85 and 95 ℃ for 15 min) on the structure and digestibility of milk protein concentrate(MPC70) was evaluated. Results shows that the free sulfhydryl content and surface hydrophobicity increased significantly with temperature up to 95 ℃, reaching the highest value of 42 μmol/L and 1 008, respectively. The contents of α-helix and β-turns decreased, while the contents of β-sheet and random coil increased. sodium dodecyl sulfate polyacrylamide gel electrophoresis after simulating gastrointestinal revealed that a certain degree of heat treatment enhanced the digestibility of milk proteins, which may be attributed to structural changes.
In this study, the effect of thermal modifications(25, 75, 85 and 95 ℃ for 15 min) on the structure and digestibility of milk protein concentrate(MPC70) was evaluated. Results shows that the free sulfhydryl content and surface hydrophobicity increased significantly with temperature up to 95 ℃, reaching the highest value of 42 μmol/L and 1 008, respectively. The contents of α-helix and β-turns decreased, while the contents of β-sheet and random coil increased. sodium dodecyl sulfate polyacrylamide gel electrophoresis after simulating gastrointestinal revealed that a certain degree of heat treatment enhanced the digestibility of milk proteins, which may be attributed to structural changes.
引文
[1]刘晓,姜竹茂,芦晶,等.热处理对牛乳蛋白质消化率的影响[J].中国乳品工业,2017,45(11):14-18.DOI:10.3969/j.issn.1001-2230.2017.11.003.
[2]盛小波,木泰华.超高压对牛乳清蛋白水解影响的研究进展[J].食品工业科技,20 1 1(10):462-466.DOI:10.13386/j.issn1002-0306.2011.10.115.
[3]仇凯,钟其顶,武金钟,等.食品中牛乳蛋白质和大豆蛋白质结构对比研究[J].中国乳品工业,2008,12(36):47-52.DOI:10.3969/j.issn.1001-2230.2008.12.013.
[4]罗永康,沈小琴,李朝慧.牛乳蛋白过敏原改性的研究[J].中国乳品工业,2005,33(10):4-8.DOI:10.3969/j.issn.1001-2230.2005.10.001.
[5]龙佩.超声波和脱酰胺改性对谷物蛋白体外消化率的影响[D].无锡:江南大学,2015:13-15.
[6]王婷婷,郭子玮,冯清妍,等.热处理对牦牛乳蛋白稳定性的影响[J].中国乳品工业,2014,42(9):4-6.DOI:10.3969/j.issn.1001-2230.2014.09.001.
[7]NUNES L,TAVARES G M.Thermal treatments and emerging technologies:impacts on the structure and techo-functional properties of milk proteins[J].Trends in Food Science and Technology,2019,90:88-99.DOI:10.1016/j.tifs.2019.06.004.
[8]BEVERIDGE T,TOMA S J,NAKA I S.Determination of SH-and SS-groups in some food proteins using Ellman's reagent[J].Journal of Food Science,2006,39(1):49-51.DOI:10.1111/j.1365-2621.1974.tb00984.x.
[9]李雪.超声波对β-乳球蛋白结构、免疫特性和美拉德反应的影响[D].南昌:南昌大学,2016:33-35.
[10]刘子华,于学玲,毛贇贇,等.SDS-聚丙烯酰胺凝胶电泳法测抗氧化低密度脂蛋白抗体的分子量[J].中国原子能科学研究院年报,2014:220-223.
[11]CONSIDINE T,PATEL H A,ANEMA S,et al.Interactions of milk proteins during heat and high hydrostatic pressure treatments:a review[J].Innovative Food Science and Emerging Technologies,2007,8:1-23.DOI:10.101 6/j.ifset.2006.08.003.
[12]JANG H D,SWAISGOOD H E.Disulfide bond formation between thermally denaturedβ-lactoglobulin andκ-casein in casein micelles[J].Journal of Dairy Science,1990,73:900-904.DOI:10.3168/jds.S0022-0302(90)78746-2.
[13]韩荣伟,王加启,郑楠.热处理对牛乳成分的变化影响及热损标识物的选择[J].中国食物与营养,2011,17(7):22-29.DOI:10.3969/j.issn.1006-9577.2011.07.007.
[14]FANG Qian,SUN Jiayue,CAO Di,et al.Experimental and modelling study of the denaturation of milk protein by heat treatment[J].Korean Journal for Food Science of Animal Resouces,2017,37(1):44-51.DOI:10.5851/kosfa.201 7.37.1.44.
[15]李雪,涂宗财,齐午成,等.超声波处理对β-乳球蛋白结构和抗原性的影响[J].食品工业科技,2016,18:106-110.DOI:10.13386/j.issn1002-0306.2016.18.012.
[16]SAVA N,VAN DER P,CLAEYS W L,et al.The kinetics of heatinduced structural changes ofβ-lactoglobulin[J].Journal ofDairy Science,2005,88(5):1646-1653.DOI:10.3168/jds.S0022-0302(05)72836-8.
[17]孙佳悦,钱方,姜淑娟,等.基于红外光谱分析热处理对牛乳蛋白质二级结构的影响[J].食品科学,2017,38(23):82-86.DOI:10.7506/spkx 1002-6630-201723014.
[18]王伟军.牛乳加热及乳粉热相关工艺对蛋白聚合及凝固特性的影响[D].哈尔滨:哈尔滨工业大学,2012:66-67.
[19]吴黎明,周群,周骁,等.蜂王浆不同贮藏条件下蛋白质二级结构的Fourier变换红外光谱研究[J].光谱学与光谱分析,2009,29(1):82-87.
[20]何光华,黄俊,尤玉茹,等.乳清蛋白的体外模拟消化过程及热处理的影响[J].中国食品学报,2012,12(4):25-29.DOI:10.16429/j.1009-7848.2012.04.015.
[21]FLORENCE B, OLIVIA M,YANN L G,et al.The heat treatment and the gelation are strong determinants of kinetics of milk proteins digestion and of the peripheral availability of amino acids[J].Food Chemistry,2013,136:1203-1212.DOI:10.1016/j.foodchem.2012.09.022.
[22]黄俊,尤玉如,肖功年,等.乳清蛋白的体外模拟消化过程及热处理的影响[J].中国食品学报,2012,12(4):25-29.DOI:10.16429/j.1009-7848.2012.04.015.
[2]盛小波,木泰华.超高压对牛乳清蛋白水解影响的研究进展[J].食品工业科技,20 1 1(10):462-466.DOI:10.13386/j.issn1002-0306.2011.10.115.
[3]仇凯,钟其顶,武金钟,等.食品中牛乳蛋白质和大豆蛋白质结构对比研究[J].中国乳品工业,2008,12(36):47-52.DOI:10.3969/j.issn.1001-2230.2008.12.013.
[4]罗永康,沈小琴,李朝慧.牛乳蛋白过敏原改性的研究[J].中国乳品工业,2005,33(10):4-8.DOI:10.3969/j.issn.1001-2230.2005.10.001.
[5]龙佩.超声波和脱酰胺改性对谷物蛋白体外消化率的影响[D].无锡:江南大学,2015:13-15.
[6]王婷婷,郭子玮,冯清妍,等.热处理对牦牛乳蛋白稳定性的影响[J].中国乳品工业,2014,42(9):4-6.DOI:10.3969/j.issn.1001-2230.2014.09.001.
[7]NUNES L,TAVARES G M.Thermal treatments and emerging technologies:impacts on the structure and techo-functional properties of milk proteins[J].Trends in Food Science and Technology,2019,90:88-99.DOI:10.1016/j.tifs.2019.06.004.
[8]BEVERIDGE T,TOMA S J,NAKA I S.Determination of SH-and SS-groups in some food proteins using Ellman's reagent[J].Journal of Food Science,2006,39(1):49-51.DOI:10.1111/j.1365-2621.1974.tb00984.x.
[9]李雪.超声波对β-乳球蛋白结构、免疫特性和美拉德反应的影响[D].南昌:南昌大学,2016:33-35.
[10]刘子华,于学玲,毛贇贇,等.SDS-聚丙烯酰胺凝胶电泳法测抗氧化低密度脂蛋白抗体的分子量[J].中国原子能科学研究院年报,2014:220-223.
[11]CONSIDINE T,PATEL H A,ANEMA S,et al.Interactions of milk proteins during heat and high hydrostatic pressure treatments:a review[J].Innovative Food Science and Emerging Technologies,2007,8:1-23.DOI:10.101 6/j.ifset.2006.08.003.
[12]JANG H D,SWAISGOOD H E.Disulfide bond formation between thermally denaturedβ-lactoglobulin andκ-casein in casein micelles[J].Journal of Dairy Science,1990,73:900-904.DOI:10.3168/jds.S0022-0302(90)78746-2.
[13]韩荣伟,王加启,郑楠.热处理对牛乳成分的变化影响及热损标识物的选择[J].中国食物与营养,2011,17(7):22-29.DOI:10.3969/j.issn.1006-9577.2011.07.007.
[14]FANG Qian,SUN Jiayue,CAO Di,et al.Experimental and modelling study of the denaturation of milk protein by heat treatment[J].Korean Journal for Food Science of Animal Resouces,2017,37(1):44-51.DOI:10.5851/kosfa.201 7.37.1.44.
[15]李雪,涂宗财,齐午成,等.超声波处理对β-乳球蛋白结构和抗原性的影响[J].食品工业科技,2016,18:106-110.DOI:10.13386/j.issn1002-0306.2016.18.012.
[16]SAVA N,VAN DER P,CLAEYS W L,et al.The kinetics of heatinduced structural changes ofβ-lactoglobulin[J].Journal ofDairy Science,2005,88(5):1646-1653.DOI:10.3168/jds.S0022-0302(05)72836-8.
[17]孙佳悦,钱方,姜淑娟,等.基于红外光谱分析热处理对牛乳蛋白质二级结构的影响[J].食品科学,2017,38(23):82-86.DOI:10.7506/spkx 1002-6630-201723014.
[18]王伟军.牛乳加热及乳粉热相关工艺对蛋白聚合及凝固特性的影响[D].哈尔滨:哈尔滨工业大学,2012:66-67.
[19]吴黎明,周群,周骁,等.蜂王浆不同贮藏条件下蛋白质二级结构的Fourier变换红外光谱研究[J].光谱学与光谱分析,2009,29(1):82-87.
[20]何光华,黄俊,尤玉茹,等.乳清蛋白的体外模拟消化过程及热处理的影响[J].中国食品学报,2012,12(4):25-29.DOI:10.16429/j.1009-7848.2012.04.015.
[21]FLORENCE B, OLIVIA M,YANN L G,et al.The heat treatment and the gelation are strong determinants of kinetics of milk proteins digestion and of the peripheral availability of amino acids[J].Food Chemistry,2013,136:1203-1212.DOI:10.1016/j.foodchem.2012.09.022.
[22]黄俊,尤玉如,肖功年,等.乳清蛋白的体外模拟消化过程及热处理的影响[J].中国食品学报,2012,12(4):25-29.DOI:10.16429/j.1009-7848.2012.04.015.
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