Ultrasonic spectrometry study of the influence of temperature on whey protein aggregation
Ultrasonic spectrometry study of the influence of temperature on whey protein aggregation
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DOI：
10.1016/s0268-005x(99)00018-1
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发表时间：
1999-11-01
影响因子：
10.7
通讯作者：
McClements, DJ
中科院分区：
文献类型：
--
作者：
Bryant, CM;McClements, DJ
采用超声衰减光谱法研究了预处理温度对天然和碱性变性乳清蛋白水溶液中ph诱导颗粒聚集体形成的影响。在2-12的pH范围内测量了2.5 wt.%乳清蛋白溶液的超声衰减光谱（1-150 MHz），使用乳清溶液，之前在30 - 90℃的温度范围内加热。在蛋白质的等电点附近（pH 3-5.5）衰减有很大的温度依赖性增加，这是由增加的蛋白质聚集引起的超声波散射引起的。在80℃时观察到最大的衰减，利用超声散射理论确定了聚集体的粒径分布和浓度。加热时检测到大颗粒（约10 μ m）的损失。超声光谱是研究溶液中蛋白质聚集的一种有价值的工具。1999爱思唯尔科学有限公司版权所有。
Ultrasonic attenuation spectroscopy was used to investigate the influence of pre treatment temperature on the formation of pH-induced particulate aggregates in aqueous native and alkaline-denatured whey protein solutions. Ultrasonic attenuation spectra (1-150 MHz) of 2.5 wt.% whey protein solutions were measured over a pH range of 2-12 using whey solutions, which were previously heated at temperatures ranging from 30 to 90 degrees C. There was a large temperature dependent increase in attenuation around the isoelectric point of the proteins (pH 3-5.5), which was caused by scattering of ultrasound by increased protein aggregation. A maximum in attenuation was observed at 80 degrees C. The particle size distribution and concentration of the aggregates was determined using ultrasonic scattering theory. A loss of large particles (similar to 10 mu m) was detected upon heating. Ultrasonic spectroscopy was shown to be a valuable tool for studying aggregation of proteins in solution. (C) 1999 Elsevier Science Ltd. All rights reserved.