Studies of the reaction between proteins and reducing sugars in the “dry” state

Aspects of calcification. The availability of ε-amino groups in collagen aggregates

“…Fraenkel-Conrat & Porter (1952) ascribed the extensive destruction of c-DNP-lysine and DNP-alanine on hydrolysis of DNP-ovomucoid to the proteinbound carbohydrate moiety. Since both the caand the c-amino groups of casein (Lea & Hannan, 1950), a-N-acetyl-L-lysine and polylysine (Hannan & Lea, 1952) react with glucose, the ac-amino group of c-DNP-lysine should also be capable of reaction with glucose or similar sugars. Gottschalk & Partridge (1950) found that free lysine reacted with glucose to yield 5-hydroxymethylfurfural derivatives, the latter rapidly forming hurmin in hot acid solution.…”

Effect of reaction conditions on product distribution from the co-pyrolysis of α-amino acids with glucose

“…While there is an abundance of literature reports on the low temperature reactions of amino acids with sugars [15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30], there is very little information on the product distribution from the copyrolysis of amino acids with sugars under conditions relevant to tobacco pyrolysis in a burning cigarette. It is not clear under what conditions the N-heterocycles or polycyclic aromatic compounds (PACs) are formed in the co-pyrolysis.…”

Isolation and characterization of pigments from protein-carbonyl browning systems. Isolation, purification, and properties

“…The early steps of the Maillard reaction are well worked out (Hodge, 1953;Reynolds, 1963Reynolds, , 1965; they involve the formation of increasingly unsaturated multi-carbonyl compounds. In dry systems and in dilute solutions containing protein, the pigment causes cross-linking between protein chains (Hannan and Lea, 1952;Mohammed et al, 1949) and thus reduced in cico and in ritro enzymatic digestibility of the protein (Ford, 1965;Ford and Salter, 1966). Lea and coworkers have studied the effects of moisture content, pH, and temperature on the reactivity of the amine groups and on the formation of color in powdered casein-glucose and milk systems such as were used in our experiments Hannan, 1949, 1950;Lea et nl., 1950).…”