Keywords

Highland Barley, Gliadin, Gluten, Gluten

Abstract

The Osbron method was used to extract gliadin and glutenin from highland barley and wheat respectively, and the four proteins were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). and infrared spectroscopy analysis, and determine its surface hydrophobicity, thermal stability, total sulfhydryl group and disulfide bond content. The results show that: the content of gliadin in highland barley protein is 16.96%, which is lower than its content in wheat protein; the content of glutenin in highland barley protein is 47.83%, which is higher than its content in wheat protein, but after SDSPAGE analysis found that the high molecular weight gluten subunit (HMW-GS) content in highland barley was much lower than that in wheat. The disulfide bond and total sulfhydryl contents in highland barley gliadin and glutenin were lower than those in wheat. There is little difference in the surface hydrophobicity of the four proteins. The thermal stability of highland barley gluten is higher than that of wheat gluten, which is not conducive to its absorption of water and partial expansion. Infrared spectroscopy analysis found that the secondary structures of wheat gliadin and highland barley gliadin are mainly composed of ¦Â-turns and ¦Â-sheets, while the proportion of ¦Â-turns in wheat gliadin is higher; highland barley glutenin and wheat glutenin The secondary structure of proteins is mainly ¦Â-sheet

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Original research done by Wu Jingjing, Wang Hongwei, Kan Jianquan

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