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首页> 外文会议>Functional properties of proteins and lipids >Thermal Denaturation and Gelation Characteristics of #beta#-Lactoglobulin Genetic Variants
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Thermal Denaturation and Gelation Characteristics of #beta#-Lactoglobulin Genetic Variants

机译：β-乳球蛋白遗传变异的热变性和凝胶化特性

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摘要

The thermal characteristics of #beta#-lactoglobulin (#beta#-lg) genetic variants A and B were studied at pH 3.0, 5.0, 7.0 and 8.0 by differential scanning calorimetry (DSC). The #beta#-lg B exhibited higher denaturation temperature and enthalpy than #beta#-lg A and also denatured in a more cooperative fashion as indicated by a lower width at half-peak height. Fourier transform infrared spectroscopy (FTIR) was used to monitor changes in secondary structure of the two proteins when heated from 25 to 95 deg C. Results showed that #beta#-lg A had a lower #beta#-sheet content than the B variant at pH 3.0 and 5.0. At pH 7.0 and 8.6 the secondary structure of the two variants were similar. Aggregation bands (1682 cm~(-1) and approx1622 cm~(-1)) were observed when the proteins were heated at all pH values. The microstructure of gels made from 10percent (w/v) solutions of #beta#-lg A and B heated at 90 deg C for 30 min was studied by electron microscopy. The gel matrix of #beta#-lg B at both acidic and alkaline pH was found to be made up of larger aggregates than the A variant. The aggregates of both variants were large (1-2 #mu#) and globular at acidic pH but much smaller (nanometer rangs) and amorphous at alkaline pH.
机译：通过差示扫描量热法（DSC）在pH 3.0、5.0、7.0和8.0下研究了＃β＃-乳球蛋白（＃β＃-lg）遗传变体A和B的热特性。 ＃beta＃-lg B比＃beta＃-lg A表现出更高的变性温度和焓，并且以更协同的方式变性，如半峰高处的较低宽度所示。当从25到95摄氏度加热时，使用傅里叶变换红外光谱（FTIR）来监视这两种蛋白质的二级结构的变化。结果显示，＃beta＃-lg A的Beta-sheet含量低于B变体在pH 3.0和5.0下。在pH 7.0和8.6下，两个变体的二级结构相似。当在所有pH值下加热蛋白质时，观察到聚集带（1682 cm〜（-1）和大约1622 cm〜（-1））。通过电子显微镜研究了由在90摄氏度加热30分钟的＃beta＃-lg A和B的10％（w / v）溶液制成的凝胶的微观结构。发现在酸性和碱性pH下，＃beta＃-lg B的凝胶基质均由比A变体更大的聚集体组成。两种变体的聚集体在酸性pH下均较大（1-2＃μ＃）和球形，而在碱性pH下则较小（纳米级）且为无定形。

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