N-Substituted lysines as sources of lysine in nutrition.

Twenty seven alpha-N- and epsilon-N-substituted derivatives of lysine belonging to eight different classes: (1) natural dipeptides, (2) alpha-N-acyl-, (3)epsilon-N-acyl-, (4)epsilon-N-(alpha-amino acyl)-, (5)epsilon-N-(omega-amino acyl)-, (6)alpha-N-epsilon-N-di-amino acyl-, (7)epsilon-N-acylglycyl- and (8)Schiff's bases were synthesized. The "in vitro" utilization of some of them was tested by a rat growth assay. Only the derivatives which provided biologically available lysine were hydrolysed by one or more of the intestinal mucosa, liver or kidney homogenates.

[Biologic availability and metabolic transit of amino acids modified by technological processing].

The biological availability of amino acids modified by industrial processes has been measured in trials on rats, and their metabolic transit (urinary and faecal excretions, transformation into CO2 and retention in organs) has been studied using molecules labelled with 14C. Maillard reaction products. epsilon-fructose-lysine is not utilized as lysine source.

[Measure of available and blocked lysine in industrial milks].

The classical methods to measure lysine availability give rise to some difficulties in milks due to the presence of deoxyketose-lysine (DOKL). Six methods, one of which measuring the blocked lysine, are studied. Amino acid chromatography gives a too high value of lysine when it is blocked as DOKL, the latter regenerating lysine during acid hydrolysis.