Deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins and reactive carbonyl groups of glyoxals (Probable). Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Thus, was shown to afford full protection against glycation of thioredoxin by glyoxal. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Prevents acrylamide formation in asparagine/glyoxal and asparagine/sugar mixtures, likely by degrading asparagine/glyoxal Maillard adducts formed at high temperatures. Also displays proteolytic activity. Cleaves at the carboxyl side of both basic and hydrophobic residues in the P1 position, indicating trypsin- and chymotrypsin-like specificities.