Casein interactions: Casting light on the black boxes, the structure in dairy products
Casein interactions: Casting light on the black boxes, the structure in dairy products
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DOI：
10.1016/s0958-6946(98)00040-5
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发表时间：
1998-03-01
影响因子：
3.1
通讯作者：
Horne, DS
中科院分区：
文献类型：
--
作者：
Horne, DS
本文综述了酪蛋白的相互作用的文献，并建议这些蛋白质的缔合状态是由吸引力的疏水相互作用和静电排斥的平衡。温度，pH值和离子强度的影响的自关联和钙诱导的聚集的个别酪蛋白的合理化，在他们的影响力的这种平衡。讨论，然后扩展到酪蛋白胶束和酪蛋白胶束的双键模型制定的相互作用的性质，反映了两种不同形式的网络中的键合的需要。该模型合理地解释了温度、pH值、离子强度、胶束离解剂和溶剂对胶束完整性的影响，即它们对力的疏水/静电平衡的影响。最后，据推测，相同类型的键合普遍存在于凝乳酶或酸化产生的酪蛋白凝胶中。然后，该模型被用来解释温度对凝乳酶凝胶强度的影响，预热对凝乳酶和牛奶的酸凝固特性的影响，以及温度对浓缩胶束悬浮液的粘弹性能的影响。(C)1998爱思唯尔科技有限公司版权所有。
This paper reviews the literature on the interactions of the caseins and suggests that the state of association of these proteins is governed by a balance of attractive hydrophobic interactions and electrostatic repulsion. The effects of temperature, pH and ionic strength on the self-association and calcium-induced aggregation of the individual caseins are rationalized in terms of their influence on this balance of forces. The discussion is then extended to the nature of the interactions prevailing in the casein micelle and a dual-bonding model of the casein micelle is formulated, reflecting the need for two different forms of bonding in the network. This model plausibly accounts for the effects of temperature, pH, ionic strength, micellar dissociating agents and solvent on the integrity of the micelle in terms of their influence on the hydrophobic/electrostatic balance of forces. Finally, it is postulated that the same type of bonding prevails in casein gels produced by renneting or acidification. The model is then used to explain the influence of temperature on rennet gel strength, the effects of forewarming on rennet and acid coagulation properties of milk, and the effect of temperature on the viscoelastic properties of a concentrated micellar suspension. (C) 1998 Elsevier Science Ltd. All rights reserved.