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 (PubMed:27530919). Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals (By similarity). Thus, was shown to afford full protection against glycation of thioredoxin by glyoxal (PubMed:27530919). Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage (By similarity). Prevents acrylamide formation in asparagine/glyoxal and asparagine/sugar mixtures, likely by degrading asparagine/glyoxal Maillard adducts formed at high temperatures (PubMed:27530919). Also displays proteolytic activity (PubMed:8626329, PubMed:16535492). Cleaves at the carboxyl side of both basic and hydrophobic residues in the P1 position, indicating trypsin- and chymotrypsin-like specificities (PubMed:16535492). H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) + L-lysyl-[protein] + lactate H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) + L-cysteinyl-[protein] + lactate H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] = glycolate + H(+) + L-arginyl-[protein] H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] = glycolate + H(+) + L-lysyl-[protein] H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] = glycolate + H(+) + L-cysteinyl-[protein] Optimum pH is 6.3 for proteolytic activity with AAF-MCA as substrate. Optimum temperature is 84-97 degrees Celsius for proteolytic activity (PubMed:8626329, PubMed:16535492). Thermostable. Displays a half-life of 19 minutes at 95 degrees Celsius (PubMed:8626329). Homooligomer (PubMed:8626329). Exists in two functional species: the predominant form is a homohexamer that comprises about 90% of the total activity, and the minor form is trimeric (PubMed:16535492). Being able to prevent acrylamide formation at 100 degrees Celsius, this enzyme could constitute a viable and unique enzymatic method to reduce acrylamide formation in food, whose presence is a worldwide concern because it is carcinogenic, reprotoxic and neurotoxic. The use of deglycases is not likely to affect the quality parameters of foods, in contrast with methods which lead to depletion of the components (asparagine and sugars) responsible for acrylamide formation. Moreover, deglycases can be used directly during the thermal process, which avoids a time consuming pre-incubation step. Consequently, many foods whose heating processes occur at around 100 degrees Celsius, such as baby foods, evaporated milk, dry soups and prune juices could be clients of the deglycase method. Belongs to the peptidase C56 family.