JA Delcour, IJ Joye, B Pareyt… - Annual review of …, 2012 - annualreviews.org
The unique properties of wheat reside primarily in its gluten-forming storage proteins. Their intrinsic viscoelastic behavior is responsible for the characteristics of different wheat-based …
Gluten protein as one of the plant resources is susceptible to genetic, physical, chemical, enzymatic and engineering modifications. Chemical modifications have myriad advantages …
SG Anema - International Dairy Journal, 2021 - Elsevier
The effects of heat on the casein proteins and the casein micelles, including their interactions with denatured whey proteins are reviewed. Aspects from chemical changes to …
For a number of applications, gluten protein polymer structures are of the highest importance in determining end‐use properties. The present article focuses on gluten protein structures …
LJ Deleu, MA Lambrecht, J Van de Vondel… - Current opinion in food …, 2019 - Elsevier
Highlights•Alkaline conditions impact on the protein structure.•Thereby influences their solubility and other techno-functional properties.•Negative nutritional effects by chemical …
L Lu, Z Yang, XN Guo, JJ Xing, KX Zhu - Food Chemistry, 2021 - Elsevier
This study investigated the influence of NaHCO 3 on the water state, gluten polymerization, microstructure and quality of frozen steamed bread dough during freeze–thaw cycles …
The impact of alkali addition on the degree of gluten polymerization and textural characteristics of textured wheat protein was investigated. Results showed that the extrusion …
Thermolysin hydrolyzates of freshly isolated, extensively stored (6 years, 6° C, dry) and heated (60 min, 90° C, in excess water) bovine serum albumin (BSA) samples were …
X Liu, YQ Huang, XW Chen, ZY Deng… - Journal of Cereal Science, 2019 - Elsevier
Zein and gliadin are both cereal proteins, indicating that they are highly compatible. In this study, gliadin was firstly added to zein to achieve different zein/gliadin ratios in aqueous …