Effects of three glutenins extracted in acidic, neutral and alkaline urea solutions on the retrogradation of wheat amylose and amylopectin

Effects of three glutenins extracted in acidic, neutral and alkaline urea solutions on the retrogradation of wheat amylose and amylopectin
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酸性、中性和碱性尿素溶液提取的三种麦谷蛋白对小麦直链淀粉和支链淀粉回生的影响

DOI:
10.1016/j.ijbiomac.2023.123576
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发表时间:
2023
影响因子:
8.2
通讯作者:
Xijun Lian
Xijun Lian
中科院分区:
化学1区
文献类型:
--
作者:
Junjie Guo;Zengfang Guo;Huaiwei Wang;Xijun Lian

文献摘要

相似文献

采用酸性、中性和碱性尿素溶液分别提取麦谷蛋白1、麦谷蛋白2和麦谷蛋白2。三种谷蛋白均富含谷氨酸(Glu,> 30%)和脯氨酸(Pro,> 20%).谷蛋白1在pH5条件下提取,其丝氨酸(Ser,5.25%)、天冬氨酸(Asp,2.99%)、酪氨酸(Tyr,3.11%)、精氨酸(Arg,2.09%)和苏氨酸(Thr,2.11%)等亲水性氨基酸含量高于其它两种蛋白。3种麦谷蛋白与直链/支链淀粉的老化结果表明,麦谷蛋白1对小麦直链淀粉的老化有明显的抑制作用。通过FT-IR、XRD、DSC和固体13 C NMR等手段对麦谷蛋白1老化后的直链淀粉进行了表征,结果表明,直链淀粉与Glu、Tyr之间形成了新的氢键,阻止了直链淀粉之间形成氢键。小麦直链淀粉中C6的某些羟基与麦谷蛋白中特定链长的Ser和Thr的某些羟基之间存在糖苷键。具有空间位阻的大分子阻碍了直链淀粉重排成规则晶体。小麦直链淀粉的回生受到抑制。本研究为控制直链淀粉的老化提供了一个关键的靶向步骤。
Three glutenins (glutenin 1, glutenin 2, and glutenin 2) were extracted in acidic, neutral and alkaline urea solutions respectively. All of the three glutenins are rich in glutamic acid (Glu, >30 %) and proline (Pro, >20 %). Glutenin 1, extracted at pH 5, shows higher contents of hydrophilic amino acids as serine (Ser, 5.25 %), aspartic acid (Asp, 2.99 %), tyrosine (Tyr, 3.11 %), arginine (Arg, 2.09 %) and threonine (Thr, 2.11 %) than the other two glutenins. The retrogradation of three glutenins with amylose/amylopectin indicated that glutenin 1 showed significant inhibition effect on the retrogradation of wheat amylose. The characterizations of amylose retrograded with glutenin 1 by FT-IR, XRD, DSC and solid13C NMR showed that new hydrogen bonds between Glu, Tyr and wheat amylose were formed, which prevented the formation of hydrogen bonds between amylose themselves. Glycosidic bonds between some hydroxyl groups of C6 in wheat amylose and certain hydroxyl groups of Ser and Thr in glutenin with specific chain length were present. The macromolecules with steric hindrance prevented the rearrangement of amylose into regular crystals. The retrogradation of wheat amylose was inhibited in this way. This study provides a key targeting step to control the retrogradation of amylose.