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27 kDa玉米γ-醇溶蛋白的半胱氨酸155是提高其体外消化率的关键氨基酸。

Cys155 of 27 kDa maize gamma-zein is a key amino acid to improve its in vitro digestibility.

作者信息

Lee Sung-Ho, Hamaker Bruce R

机构信息

Department of Food Science, Purdue University, West Lafayette, IN 47907-2009, USA.

出版信息

FEBS Lett. 2006 Oct 30;580(25):5803-6. doi: 10.1016/j.febslet.2006.09.033. Epub 2006 Sep 27.

Abstract

Twenty-seven kilodalton gamma-zein is a subclass of the maize zein storage proteins and, due to its localization at the protein body periphery, is critical to digestibility characteristics of all zeins. This protein had low in vitro digestibility, presumably due to its high Cys content (7.35 mol%) that is similar to the hard-to-digest analogous sorghum protein, gamma-kafirin. Therefore, each of the conserved disulfide-bonded Cys' was mutated to create C144A, C148A, C155A, and C156A maize gamma-zein mutants. The C155A showed a remarkable increase in digestibility to proteases - pepsin, chymotrypsin, and trypsin. A high conservation of this Cys among cereal gamma-prolamins indicates the utility of this finding.

摘要

27千道尔顿的γ-玉米醇溶蛋白是玉米醇溶蛋白储存蛋白的一个亚类,由于其位于蛋白体周边,对所有玉米醇溶蛋白的消化特性至关重要。这种蛋白质的体外消化率较低,可能是由于其高半胱氨酸含量(7.35摩尔%),这与难以消化的类似高粱蛋白γ-高粱醇溶蛋白相似。因此,将每个保守的二硫键连接的半胱氨酸进行突变,以创建C144A、C148A、C155A和C156A玉米γ-玉米醇溶蛋白突变体。C155A对蛋白酶——胃蛋白酶、胰凝乳蛋白酶和胰蛋白酶的消化率显著提高。谷物γ-醇溶蛋白中这个半胱氨酸的高度保守表明了这一发现的实用性。

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