详细信息
Protein aggregation behavior during highland barley dough formation induced by different hordein/glutelin ratio ( SCI-EXPANDED收录 EI收录)
文献类型:期刊文献
英文题名:Protein aggregation behavior during highland barley dough formation induced by different hordein/glutelin ratio
作者:Liu, Xinyue[1,2];Duan, Hao[1];Liu, Gaigai[1];Liang, Wei[2];Zhao, Wenqing[2];Zheng, Jiayu[2];Li, Wenhao[2];Yan, Wenjie[1]
第一作者:Liu, Xinyue
通讯作者:Yan, WJ[1]
机构:[1]Beijing Union Univ, Beijing Key Lab Bioact Subst & Funct Foods, Beijing 100023, Peoples R China;[2]Northwest A&F Univ, Coll Food Sci & Engn, Engn Res Ctr Grain & Oil Functionalized Proc Univ, 22 Xinong Rd, Yangling 712100, Shaanxi, Peoples R China
第一机构:北京联合大学应用文理学院|北京联合大学生物化学工程学院
通讯机构:[1]corresponding author), Beijing Union Univ, Beijing Key Lab Bioact Subst & Funct Foods, Beijing 100023, Peoples R China.|[114172]北京联合大学应用文理学院;[11417]北京联合大学;[1141726]北京联合大学生物化学工程学院;
年份:2025
卷号:465
外文期刊名:FOOD CHEMISTRY
收录:;EI(收录号:20244717392648);Scopus(收录号:2-s2.0-85209241755);WOS:【SCI-EXPANDED(收录号:WOS:001362907200001)】;
基金:This study was financially supported by the National Natural Science Foundation of China (No. 32172244) .
语种:英文
外文关键词:Model dough; Hordein-glutelin structural information; Rheology; Moisture distribution; Behavioural functionalization
摘要:To investigate why highland barley dough cannot form a gluten structure, the mechanism by which the ratio of hordein/glutelin affects protein aggregation behavior during the formation of barley dough was investigated. It was observed that the pasting properties of the reconstituted flour were markedly diminished (1154-1303 x 10-3 Pa center dot s). The 50Hordein-50Glutelin sample exhibited the highest farinograph quality number. The K, A22 (48.82-65.26 %), hardness, free -SH (0.76 %-0.95 %), random coil, and hydrogen bonding (0.091-0.179 g/100 g) exhibited a notable increase with a reduction in the hordein/glutelin ratio. Conversely, beta-sheet (27.39 %- 40.11 %) and fluorescence intensity declined pronouncedly. The 50H-50G facilitated the reinforcement of protein crosslinking and polymerization, enhanced the continuity and order of the protein network structure, and further augmented the dough's viscoelasticity. The results would regulate the macroscopic quality of barley and other miscellaneous grain products through endogenous components, establishing a foundation for enhancing their quality.
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