Alimentary Analysis Unit, National Engineering School of Sfax, BPW 3038, Sfax, Tunisia; Montpellier University, UMR IATE, Place E. Bataillon, 34095 Montpellier Cedex 5, France.
Montpellier University, UMR IATE, Place E. Bataillon, 34095 Montpellier Cedex 5, France.
Colloids Surf B Biointerfaces. 2017 Aug 1;156:55-61. doi: 10.1016/j.colsurfb.2017.05.002. Epub 2017 May 2.
The effect of pH (4.3 or 6.5) and heat treatment (70°C or 90°C for 30min) on the foaming and interfacial properties of α-lactalbumin extracted from camel milk were studied. The increased temperature treatment changed the foaming properties of camel α-lactalbumin solution and its ability to unfold at the air-water interface. At neutral pH, heat treatment was found to improve foamability, whereas at acid pH (4.3) this property decreased. Foams were more stable after a heat treatment at pH 4.3 than at 6.5, due to higher levels of protein aggregation at low pH. Heat treatment at 90°C for 30min affected the physicochemical properties of the camel α-lactalbumin by increasing free thiol group concentration at pH 6.5. Heat treatment also caused changes in α-lactalbumin's surface charge. These results also confirm the pronounced aggregation of heated camel α-lactalbumin solution at acid pH.
研究了 pH 值（4.3 或 6.5）和热处理（70°C 或 90°C 30min）对骆驼乳中提取的α-乳白蛋白起泡和界面性能的影响。升高的温度处理改变了骆驼α-乳白蛋白溶液的起泡性能及其在气-水界面展开的能力。在中性 pH 下，热处理被发现可提高泡沫性能，而在酸性 pH（4.3）下，该性能降低。在 pH 4.3 下进行热处理后，泡沫更稳定，这是由于在低 pH 值下蛋白质聚集程度更高。在 90°C 下热处理 30min 会通过增加 pH 值为 6.5 时的游离巯基浓度来影响骆驼α-乳白蛋白的物理化学性质。热处理还导致α-乳白蛋白表面电荷发生变化。这些结果还证实了在酸性 pH 值下加热的骆驼α-乳白蛋白溶液明显聚集。
