“…Such modifications can be covalent (such as fragmentation, hydrolysis, deamidation, imide formation, isomerization, racemization, transpeptidation, disulfide scission/reduction/formation, thiol-disulfide exchange, oxidation and aggregation) as well as non-covalent (such as denaturation, misfolding, adsorption, aggregation and precipitation). Certain amino acids may also react with aldehydic (reducing) sugars, producing a various range of different Maillard browning reactions (Dworschak, 1980;Friedman et al, 1984). Several of these abundantly occurring modifications are detrimental for protein digestibility, especially if the protein sources have been through previous heat treatments before extrusion.…”