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CHARACTERISATION AND FUNCTIONAL STUDIES OF RICE PROTEINS

机译:水稻蛋白的特征与功能研究

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Rice is one of the most important crops all over the world. However, dough-making quality of rice storage proteins is very poor compared to wheat. Structure and properties of the storage proteins of wheat and rice are significantly different. The storage protein composition of rice shows more similarities to legume proteins than to wheat, barley and rye. While the most abundant storage proteins are member of the prolamin family in cereals, the major protein components in rice, called glutelin, belongto the globulin group. Glutelins the major rice storage proteins are soluble in diluted acid or alkaline solution. The subunits are able to form large macromolecule complexes stabilised by disulfide bonds and hydrophobic interactions (Utsumi, 1992). Itwas assumed that besides hydrogen and disulfide bonding extensive aggregation and glycosylation may also be partly responsible for the limited solubility of the rice polymeric glutelin fraction. Rice glutelins are synthesized as precursor polypeptides, which are posttranslationally cleaved into two smaller subunits.
机译:大米是世界上最重要的作物之一。然而,与小麦相比,水稻储存蛋白的面团质量非常差。小麦和水稻储存蛋白的结构和性质显着不同。水稻的储存蛋白质组成显示与豆类蛋白质的更多相似性,而不是小麦,大麦和黑麦。虽然最丰富的储存蛋白质是谷物中果冻家族的成员,而米尔的主要蛋白质成分,称为胶林蛋白,属于球蛋白组。胶林蛋白主要水稻储存蛋白质可溶于稀释的酸或碱性溶液中。亚基能够形成通过二硫键和疏水相互作用稳定的大型大分子配合物(UTSumi,1992)。假设ITWAS除了氢和二硫键外,含有巨大的聚集和糖基化也可以部分地负责水稻聚合物胶质蛋白级分的有限溶解度。将米胶林素合成为前体多肽,其后期裂解成两个较小的亚基。

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