Monahan F J, McClements D J, German J B
Department of Food Science, University College, Dublin, Belfield, Ireland.
Adv Exp Med Biol. 1997;415:127-36. doi: 10.1007/978-1-4899-1792-8_10.
The effects of protein polymerization in whey protein isolate-stabilized emulsions on emulsion properties were investigated. Polymerization, involving intermolecular disulfide bonds between whey proteins adsorbed at the oil-water interface, increased with increasing storage time following emulsion formation. Ageing resulted in increased aggregation of emulsion droplets, emulsion viscosity and susceptibility to creaming but these effects were lower when thiol-disulfide interchange reactions were inhibited by N-ethylmaleimide (NEM). Following heating to 75 degrees C, disulfide-mediated polymerization of whey proteins increased as did droplet aggregation, emulsion viscosity and creaming. While NEM lowered the extent of disulfide-mediated polymerization it did not affect the measured physical properties of the heated emulsions. Non-covalent interactions appeared to be the principal forces leading to aggregation of emulsion droplets but aggregates once formed were stabilized by disulfide bonds.
研究了乳清分离蛋白稳定乳液中蛋白质聚合对乳液性质的影响。聚合作用涉及吸附在油水界面的乳清蛋白之间的分子间二硫键,在乳液形成后的储存时间增加时会增强。老化导致乳液滴的聚集增加、乳液粘度增加以及乳析敏感性增加,但当巯基 - 二硫键交换反应被N - 乙基马来酰亚胺(NEM)抑制时,这些影响会降低。加热至75摄氏度后,乳清蛋白的二硫键介导的聚合增加,乳液滴聚集、乳液粘度和乳析也增加。虽然NEM降低了二硫键介导的聚合程度,但它不影响加热乳液的测量物理性质。非共价相互作用似乎是导致乳液滴聚集的主要力量,但一旦形成聚集体,就会通过二硫键稳定下来。