Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10894763 | Trends in Food Science & Technology | 2015 | 10 Pages |
Abstract
A more structure-ordered, homogeneous and elastic gluten network is formed at the optimum mixing stage as a consequence of glutenin and gliadin interactions. Comparative studies in different model systems demonstrate that further frozen storage exerts detrimental effects on gluten proteins in diverse ways from both gluten proteins-water interactions and structure-functionality perspectives.
Keywords
HMSGSHRP-HPLCGMPTD-NMRCLSMLMSΔHSEC-MALLSTime-domain nuclear magnetic resonanceSDSmaximum resistance to extensioncentral domainDSCG″G′Amino acidsSDS-PAGESodium dodecyl sulfate polyacrylamide gel electrophoresisTemLoss tangentDisulphideFrozen storageMelting enthalpyLow molecular weight glutenin subunitssodium dodecyl sulfateFTIRFourier transform infrared spectroscopyGlutenin macropolymerSEMElastic moduluscomplex modulusviscous modulusScanning electron microscopyTransmission electron microscopyconfocal laser scanning microscopyHigh molecular weight glutenin subunitsMolecular weightGluten proteinsDifferential scanning calorimetryreversed-phase high-performance liquid chromatographyGlutathione
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Authors
Pei Wang, Zhengyu Jin, Xueming Xu,