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Characterization of casein and alpha lactalbumin of African elephant (Loxodonta africana) milk

机译:非洲象(Loxodonta africana)牛奶中酪蛋白和α乳清蛋白的表征

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摘要

The current research reports partial characterization of the caseins and α-lactalbumin (α-LA) of the African elephant with proposed unique structure-function properties. Extensive research has been carried out to understand the structure of the casein micelles. Crys-tallographic structure elucidation of caseins and casein micelles is not possible. Consequently, several models have been developed in an effort to describe the casein micelle, specifically of cow milk. Here we report the characterization of African elephant milk caseins. The k-caseins and β-caseins were investigated, and their relative ratio was found to be approximately 1:8.5, whereas α-caseins were not detected. The gene sequence of β-casein in the NCBI database was revisited, and a different sequence in the N-terminal region is proposed. Amino acid sequence alignment and hydropathy plots showed that the k-casein of African elephant milk is similar to that of other mammals, whereas the 3-casein is similar to the human protein, and displayed a section of unique AA composition and additional hydrophilic regions compared with bovine caseins. Elephant milk is destabilized by 62% alcohol, and it is speculated that the β-casein characteristics may allow maintenance of the colloidal nature of the casein micelle, a role that was previously only associated with k-casein. The oli-gosaccharide content of milk was reported to be low in dairy animals but high in some other species such as humans and elephants. In the milk of the African elephant, lactose and oligosaccharides both occur at high levels. These levels are typically related to the content of α-LA in the mammary gland and thus point to a specialized carbohydrate synthesis, where the whey protein α-LA plays a role. We report the characterization of African elephant α-LA. Homology modeling of the α-LA showed that it is structurally similar to crystal structures of other mammalian species, which in turn may be an indication that its functional properties, such as lactose synthesis, should not be impaired.
机译:当前的研究报道了非洲大象的酪蛋白和α-乳白蛋白(α-LA)的部分表征,并提出了独特的结构功能特性。已经进行了广泛的研究以了解酪蛋白胶束的结构。酪蛋白和酪蛋白胶束的晶体结构不可能阐明。因此,已经开发了几种模型来描述酪蛋白胶束,特别是牛奶中的酪蛋白胶束。在这里,我们报告非洲大象牛奶酪蛋白的表征。研究了k-酪蛋白和β-酪蛋白,它们的相对比例约为1:8.5,而未检测到α-酪蛋白。回顾了NCBI数据库中β-酪蛋白的基因序列,并提出了N端区域的其他序列。氨基酸序列比对和亲水性图显示,非洲象奶的k-酪蛋白与其他哺乳动物的k-酪蛋白相似,而3-酪蛋白与人的蛋白质相似,并显示出一部分独特的AA组成和其他亲水区域与牛酪蛋白。象奶被62%的酒精破坏了稳定性,推测β-酪蛋白的特性可以维持酪蛋白胶束的胶体性质,而以前只与k-酪蛋白有关。据报道,奶牛动物的牛奶中低聚糖含量较低,而其他一些物种(例如人类和大象)中的寡糖含量较高。在非洲象的牛奶中,乳糖和低聚糖都大量存在。这些水平通常与乳腺中α-LA的含量有关,因此指向专门的碳水化合物合成,乳清蛋白α-LA在其中起作用。我们报告了非洲大象α-LA的表征。对α-LA的同源性建模表明,其结构与其他哺乳动物物种的晶体结构相似,这反过来可能表明它的功能特性(如乳糖合成)不应受到损害。

著录项

  • 来源
    《Journal of dairy science》 |2015年第12期|8308-8318|共11页
  • 作者单位

    Department of Microbial, Biochemical and Food Biotechnology, University of the Free State, PO Box 339, Bloemfontein 9300, Republic of South Africa;

    Department of Microbial, Biochemical and Food Biotechnology, University of the Free State, PO Box 339, Bloemfontein 9300, Republic of South Africa;

    Department of Microbial, Biochemical and Food Biotechnology, University of the Free State, PO Box 339, Bloemfontein 9300, Republic of South Africa;

    Department of Microbial, Biochemical and Food Biotechnology, University of the Free State, PO Box 339, Bloemfontein 9300, Republic of South Africa;

    UMR 1313 Genetique Animale et Biologie Integrative, Institut National de la Recherche Agronomique, Domaine de Vilvert - Batiment 221, 78350 Jouy-en-Josas, France;

    Department of Microbial, Biochemical and Food Biotechnology, University of the Free State, PO Box 339, Bloemfontein 9300, Republic of South Africa;

  • 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

    African elephant; milk; casein; α-lactalbumin; protein structure;

    机译:非洲象牛奶;酪蛋白α-乳清蛋白;蛋白质结构;
  • 入库时间 2022-08-17 23:23:45

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