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Invited review: Caseins and the casein micelle: Their biological functions, structures, and behavior in foods

机译:特邀评论:酪蛋白和酪蛋白胶束:它们在食品中的生物学功能,结构和行为

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摘要

A typical casein micelle contains thousands of casein molecules, most of which form thermodynamically stable complexes with nanoclusters of amorphous calcium phosphate. Like many other unfolded proteins, caseins have an actual or potential tendency to assemble into toxic amyloid fibrils, particularly at the high concentrations found in milk. Fibrils do not form in milk because an alternative aggregation pathway is followed that results in formation of the casein micelle. As a result of forming micelles, nutritious milk can be secreted and stored without causing either pathological calcification or amyloidosis of the mother's mammary tissue. The ability to sequester nanoclusters of amorphous calcium phosphate in a stable complex is not unique to caseins. It has been demonstrated using a number of noncasein secreted phosphoproteins and may be of general physiological importance in preventing calcification of other biofluids and soft tissues. Thus, competent noncasein phosphoproteins have similar patterns of phosphoryla-tion and the same type of flexible, unfolded conformation as caseins. The ability to suppress amyloid fibril formation by forming an alternative amorphous aggregate is also not unique to caseins and underlies the action of molecular chaperones such as the small heat-shock proteins. The open structure of the protein matrix of casein micelles is fragile and easily perturbed by changes in its environment. Perturbations can cause the polypeptide chains to segregate into regions of greater and lesser density. As a result, the reliable determination of the native structure of casein micelles continues to be extremely challenging. The biological functions of caseins, such as their chaperone activity, are determined by their composition and flexible conformation and by how the casein polypeptide chains interact with each other. These same properties determine how caseins behave in the manufacture of many dairy products and how they can be used as functional ingredients in other foods.
机译:典型的酪蛋白胶束包含数千个酪蛋白分子,其中大多数与无定形磷酸钙纳米簇形成热力学稳定的复合物。像许多其他未折叠的蛋白质一样,酪蛋白具有组装成有毒性的淀粉样原纤维的实际或潜在趋势,尤其是在牛奶中发现的高浓度下。牛奶中不形成原纤维,因为遵循替代的聚集途径,导致酪蛋白胶束的形成。由于形成胶束,可以分泌和储存营养乳,而不会引起母亲乳腺组织的病理性钙化或淀粉样变性。螯合稳定复合物中无定形磷酸钙纳米簇的能力不是酪蛋白独有的。已经证明使用许多非酪蛋白分泌的磷蛋白,并且在防止其他生物流体和软组织钙化方面可能具有一般的生理重要性。因此,有能力的非酪蛋白磷酸蛋白具有与酪蛋白相似的磷酸化模式和相同类型的柔性,未折叠构象。通过形成替代的无定形聚集体来抑制淀粉样蛋白原纤维形成的能力也不是酪蛋白独有的,并且是诸如小热激蛋白之类的分子伴侣的作用的基础。酪蛋白胶束的蛋白质基质的开放结构易碎,并且容易受到其环境变化的干扰。扰动可能导致多肽链分离成密度更大或更小的区域。结果,酪蛋白胶束天然结构的可靠测定仍然极具挑战性。酪蛋白的生物学功能,例如其伴侣活性,取决于它们的组成和柔性构象,以及酪蛋白多肽链如何相互作用。这些相同的特性决定了酪蛋白在许多乳制品生产中的行为方式以及它们如何用作其他食品中的功能成分。

著录项

  • 来源
    《Journal of dairy science》 |2013年第10期|6127-6146|共20页
  • 作者单位

    Institute of Molecular, Cell and Systems Biology, School of Life Sciences, University of Glasgow, Glasgow G12 8QQ, United Kingdom;

    School of Chemistry and Physics, The University of Adelaide, Adelaide, SA 5005, Australia,Research School of Chemistry, College of Physical and Mathematical Sciences, The Australian National University, Canberra, ACT 0200, Australia;

    School of Biological Sciences and Illawarra Health and Medical Research Institute, University of Wollongong, Wollongong, NSW 2522, Australia;

    Centre for Protein Engineering, University of Liege, 4000 Liege, Belgium;

  • 收录信息 美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    unfolded protein; molecular chaperone; calcium phosphate sequestration; amyloid fibril;

    机译:展开的蛋白质分子伴侣磷酸钙螯合;淀粉样原纤维;
  • 入库时间 2022-08-17 23:24:16

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