Journal of Dairy Research · 1977 · 13 citations · 5 references
AgricultureBiochemistryFood ScienceFood ChemistryMilk ChemistryMilk CompositionCasein ChemistryHeat Treatment Of MilkMilk ProteinsPhysicochemical Properties Of MilkAcidity Changes During Heat TreatmentAcidity In Uht MilkHydrolysisMaillard Reaction In MilkMilk Heat Treatment EffectsMilk Heat-induced ChangesMilk Protein CharacterizationMilk Protein Hydrolysates
Summary Four chemical methods were used in a comparison of the measurement of the extent of modification of lysine residues in casein during storage of ultra-heat-treated (UHT) milk. Determination of homoarginine after reaction with o -methylisourea appeared to be the best measure of total lysine modification. Reduction with borohydride before acid hydrolysis prevented recovery of lysine from lactuloselysine (ε- N -deoxylactulosyl-L-lysine) and fructoselysine (ε- N -deoxyfructosyl-L-lysine). This procedure gave values for these derivatives which were in good agreement with those obtained from the determination of furosine (ε- N -(2-furoylmethyl)-L-lysine) in acid hydrolysates. Determination of lysine after acid hydrolysis showed that lysine loss was accounted for by lactuloselysine and fructoselysine formation in most of the samples. Browning was most apparent in UHT milk stored at 37 °C for 3 years and in this sample only part of the lysine residues was accounted for as lactuloselysine and fructoselysine, thus indicating that lysine had become involved further in sugar degradation products.
5
Mechanisms of heat damage in proteins
Richard F. Hurrell, K. J. Carpenter, William John Sinclair et al. · British Journal Of Nutrition · 1976 · 202 citations · Full text
Mechanisms of heat damage in proteins
Richard F. Hurrell, K. J. Carpenter · British Journal Of Nutrition · 1974 · 95 citations · Full text