热加工对乳清中主要过敏原潜在致敏性的影响
目的 探讨不同温度条件下, 热加工对牛乳中主要过敏原潜在致敏性的影响。方法 将α-乳白蛋白与β-乳球蛋白经不同的加热条件处理后, 用间接ELISA检测上述2种过敏原蛋白IgG的结合能力的变化。结果 热处理后的α-乳白蛋白的IgG结合能力呈上升趋势; 但经60~75 ℃热处理的α-乳白蛋白均比未加工的抗原性低, 经60 ℃热处理的α-乳白蛋白的IgG结合能力下降幅度最大, 下降比例为40%; 经80 ℃热处理的α-乳白蛋白IgG结合能力大于未处理的α-乳白蛋白。热处理对β-乳球蛋白的IgG结合能力的影响与α-乳白蛋白相反: 在60~80 ℃热加工条件下, β-乳球蛋白的抗原性随着温度的升高, 抗原性逐渐减小, 且经80 ℃加热处理的β-乳球蛋白的IgG结合能力最低, 但仍然大于未加工的β-乳球蛋白的IgG结合能力。结论 热加工能改变α-乳白蛋白和β-乳球蛋白IgG结合能力, 进而改变致敏性。
Objective To investigate the effect of thermal processing on the potential allergenicity of major allergens in milk under different temperature conditions. Methods The binding ability of α-lactalbumin and β-lactoglobulin after treated with different heating conditions to IgG was detected by ELISA. Results The results showed that the binding ability of α-lactalbumin to IgG after thermal processing was increased, but the binding ability of α-lactalbumin treated at 60~75 ℃ was lower than that of untreated antigen. The binding ability of α-lactalbumin to IgG after treated at 60 ℃ was the largest while decreased by 40% compared with untreated antigen. The binding ability of α-lactalbumin to IgG after treated at 80 ℃ was bigger than untreated α-lactalbumin. It was opposite that the effect of thermal processing on the binding ability of β-lactoglobulin to IgG compared with α-lactalbumin: with the increase of temperature, the antigenicity of β-lactoglobulin decreased at 60~80 ℃, while the binding ability of β-lactoglobulin after treated at 80 ℃ was the lowest but still bigger than that of untreated β-lactoglobulin. Conclusion Thermal processing can change the binding ability of α-lactalbumin and β-lactoglobulin to IgG, and then change the sensitization.
标题:热加工对乳清中主要过敏原潜在致敏性的影响
英文标题:Effects of thermal processing on the potential allergenicity of major allergens in whey
作者:
费爽雯 南昌大学食品科学与技术国家重点实验室
白浩 南昌大学食品科学与技术国家重点实验室
李欣 南昌大学食品科学与技术国家重点实验室
曾弘华 江西省丰城市剑光医院
陈红兵 南昌大学食品科学与技术国家重点实验室,南昌大学中德研究院
李守明 江西省儿童医院
中文关键词:热加工,牛乳过敏原,α-乳白蛋白,β-乳球蛋白,
英文关键词:thermal processing,milk allergens,α- lactalbumin,β-lactoglobulin,
发表日期:2017-01-15
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- 25.69 MB
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