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Cited by 35 publications
(22 citation statements)
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“…These results suggested that heat treatment may have caused decomposition of proteins and peptides 9 . Different degrees of decline in the free amino acids occurred in the heat treatment because the Maillard reaction involves amino acids and peptides as reactants to react with reducing sugars to form various substances 10,22 …”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…These results suggested that heat treatment may have caused decomposition of proteins and peptides 9 . Different degrees of decline in the free amino acids occurred in the heat treatment because the Maillard reaction involves amino acids and peptides as reactants to react with reducing sugars to form various substances 10,22 …”
Section: Resultsmentioning
confidence: 99%
“…These results suggested that heat treatment may have caused decomposition of proteins 9 Different degrees of decline in the free amino acids occurred in the heat treatment because the Maillard reaction involves amino acids and peptides as reactants to react with reducing sugars to form various substances. 10,22 Histidine, arginine, tyrosine, valine, lysine, isoleucine, leucine, phenylalanine and tryptophan were present in higher amounts in unheated controls, accounting for approximately 55% of total amino acids detected. These amino acids are considered as 'bitter' tasting amino acids.…”
Section: Changes Of Ph and Reducing Sugar Contentsmentioning
confidence: 98%
“…Generally, the balance between hydrophilic and hydrophobic groups determines the structure of a protein. Its stability largely depends on the hydrophobic interactions within the molecule (Nooshkam & Varidi, 2020). As an example, adding Dex and SA molecules with strong hydrophilicity to BBP offsets the hydrophilichydrophobic balance of the BBP, causing the number of hydrophilic groups in the BBP peptide chain to increase and ultimately enhancing the hydrophilicity of the molecular surface (Weng et al, 2016).…”
Section: Surface Hydrophobicitymentioning
confidence: 99%
“…Whey protein isolate (WPI) is extensively used as an emulsifier in the formulation of food emulsions. This ingredient contains a mixture of globular milk proteins that can retard lipid oxidation in emulsions because of their ability to scavenge free radicals and chelate metal ions 18 . In addition, WPI can act as a thickening or gelling agent because of its ability to unfold and aggregate when heated above its thermal denaturation temperature (around 65 °C).…”
Section: Introductionmentioning
confidence: 99%
“…This ingredient contains a mixture of globular milk proteins that can retard lipid oxidation in emulsions because of their ability to scavenge free radicals and chelate metal ions. 18 In addition, WPI can act as a thickening or gelling agent because of its ability to unfold and aggregate when heated above its thermal denaturation temperature (around 65 °C). Previous studies have focused on the impact of polysaccharides, including KGM, xanthan gum and galactomannan cassia gum, on the gelling properties of whey proteins.…”
Section: Introductionmentioning
confidence: 99%