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麦谷蛋白

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The properties of isoelectric points of high-molecular-weight glutenin subunits in five varieties of common wheat and one variety of durum wheat were studied by two double-way electrophoresis techniques, IEF×SDS-PAGE and NEPEGE×PAGE.

运用IEF×SDS-PAGE和NEPEGE×PAGE2种双向电泳技术对5个普通小麦品种和1个硬粒小麦品种的高分子量麦谷蛋白亚基等电点的特性进行了研究。

The composition and structure of vital wheat gluten ,which contains the gluten in and gliadin subunits,were reviewed in great detail in the paper.

详细介绍了小麦面筋蛋白中麦谷蛋白和醇溶蛋白的亚基组成和结构,以及各亚基与面团品质的关系。

The results showed that the treatment of nitrogen and sulfur fertilizer obviously affect wheat protein and glutenin macropolymer.

结果表明:氮肥与硫肥的不同处理对小麦籽粒的蛋白质和麦谷蛋白大聚合体有明显影响。

The differences between raw material and instruments, which were used during testing glutenin, were analyzed.

这些内容对根据实际实验条件和工作需要,选择适当麦谷蛋白研究的方法提供信息。

High molecular weight glutenin subunits are one group of the major components of storage proteins in wheat seeds.

高分子量麦谷蛋白是小麦籽粒贮藏蛋白的重要组分。

Glutenin is the one of major components of the storage protein in wheat and a significant contribution to dough rheology and baking quality.

麦谷蛋白是小麦贮藏蛋白的主要组成成分之一,决定面团的强度和面包的烘烤品质。

The composition of high-molecular-weight glutenin subunits in 360 varieties were analyzed by using SDS-PAGE method in this experiment.

应用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳方法,分析了360份甘肃省冬小麦资源的高分子量麦谷蛋白亚基组成。

In the protein of barley, the contents of Glu, Pro, Phe, Arg are high, and the Limitation amino acids are Met and Trp. The content of Lys in barley is higher than that in wheat, which showed it had a good nutrition quality. The reason for barley protein unforms gluten net tissue was the content less of prolamine and glutein in the protein of barley. The one of main factors for barley showing high biological activity functions might lie in its high β-glucan and polyphenol chemical compound content.

大麦蛋白质中谷氨酸、脯氨酸、苯丙氨酸和精氨酸含量较高,限制性氨基酸为蛋氨酸和色氨酸,赖氨酸的含量高于小麦的,表现出较好的营养品质;大麦蛋白质组分中醇溶蛋白和麦谷蛋白含量较低,是其不能形成面筋网络组织的主要原因;大麦中含有β-葡聚糖和多酚类化合物是其生理活性功能较强的主要因素之一。

The principle of protein's influencing on qualities of the both noodles is, glutenin and gliadin give the dough with shapeable ability by forming net construction of gluten; and give cooked dried noodle and instant noodle with hardness, extending ability and part of springiness by coagulating with each other when they are heated.

蛋白质对于挂面及方便面品质的影响机理在于:麦谷蛋白和醇溶蛋白通过形成面筋的网络结构,赋予面团以成形性;通过受热产生凝集变性,赋予面条以筋力、硬度和部分弹性。

The results indicated that AX interacted with glutenin by covalently bond FA to tyrosine of glutenin.

结果表明AX与面筋蛋白的相互作用主要是由AX分子侧链上的阿魏酸与麦谷蛋白分子上的酪氨酸基团相互作用引起的。

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