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中国精品科技期刊2020
李雪, 涂宗财, 齐午城, 王辉, 杨文华, 田明. 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
引用本文: 李雪, 涂宗财, 齐午城, 王辉, 杨文华, 田明. 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
LI Xue, TU Zong-cai, QI Wu-cheng, WANG Hui, YANG Wen-hua, TIAN Ming. Effect of ultrasound treatment on structure and antigenicity of β- lactoglobulin[J]. Science and Technology of Food Industry, 2016, (18): 106-110. DOI: 10.13386/j.issn1002-0306.2016.18.012
Citation: LI Xue, TU Zong-cai, QI Wu-cheng, WANG Hui, YANG Wen-hua, TIAN Ming. Effect of ultrasound treatment on structure and antigenicity of β- lactoglobulin[J]. Science and Technology of Food Industry, 2016, (18): 106-110. DOI: 10.13386/j.issn1002-0306.2016.18.012

超声波处理对β-乳球蛋白结构和抗原性的影响

Effect of ultrasound treatment on structure and antigenicity of β- lactoglobulin

  • 摘要: 采用电泳、圆二色谱、荧光光谱及酶联免疫吸附等方法,研究了超声波处理对β-乳球蛋白(β-lactoglobulin,β-Lg)结构和抗原性的影响。结果表明:随着超声波功率的增大,β-Lg的分子量无显著性变化,自由巯基含量下降,β-折叠含量和表面疏水性呈先升高后降低的趋势,且均在400 W时达到最大值。这表明超声波处理能迫使β-Lg结构展开,破坏其高级结构。与此同时,β-Lg的抗原性呈先升高后降低的趋势,在400 W 25 min时达到最大,为2540.20μg/m L,比未处理样品增加了133%,这表明β-Lg结构的展开可能会导致其过敏表位的暴露,因此,β-Lg抗原性的改变可能与其高级结构的变化有关。 

     

    Abstract: In order to study the effect of ultrasound treatment on structure and antigenicity of β- lactoglobulin( β-Lg),SDS-PAGE,circular dichroism spectra,fluorescence spectrum and indirect competitive enzyme- linked immunosorbent assay were used to measure the structure and antigenicity,respectively. The molecular weight ofβ- Lg was not significant change,free sulfhydryl groups decreased,the content of β- sheet and surface hydrophobicity firstly increased and then decreased with the increasing of ultrasonic power.The content of β- sheet and surface hydrophobicity reached the maximum with 400 W ultrasound treatment. It was indicated that β- Lg could be unfolded and spacial structure was destroyed by ultrasound treatment. Meanwhile,the antigenicity ofβ- Lg was also firstly increased and then decreased. When it was treated at 400 W for 25 min,the antigenicity ofβ- Lg increased up to 2540.20 μg / m L,showing an increase by 133%. The results indicated that the unfolding ofβ- Lg might result in the allergic epitope exposed.Therefore,the antigenicity change of β- Lg was probably related to its spacial structural alteration induced by ultrasound treatment.

     

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