The low molecular weight fraction of a glucose-lysine reaction mixture, previously shown to affect the in vivo uptake of proteins in the rat, was tested for its effect on a number of gastrointestinal proteases and peptidases in vitro. Of these, carboxypeptidase A was significantly inhibited by 0.5 mg/mL of the Maillard products, and aminopeptidase N (a key enzyme in the brush border hydrolysis of peptides) was strongly inhibited by 0.25 mg/mL. The inhibition of aminopeptidase N was of the mixed type while the inhibition of carboxypeptidase A could not be described by means of classical enzyme kinetics. Gel filtration chromatography indicated that a number of different compounds in the Maillard reaction mixture may inhibit the two enzymes.

Zindler-Frank, E. "Oxalate Biosynthesis in Relation to Photosynthetic Pathway and Plant Producticity-A Survey". Z. Pflanzenphysiol. 1976, 80, 1-13.

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