Peptidoglutaminase deamidation of proteins and protein hydrolysates for improved food use

Abstract The limited deamidating ability of peptidoglutaminase (PGase) toward intact food proteins (0‐ 6% deamidation) can be significantly enhanced by prior protein hydrolysis and altering protein conformation by such means as moist heat. PGase deamidation increases protein solubility and improves emulsifying and other physical properties under mildly acidic conditions. A batch reactor method was developed for the large‐ scale PGase deamidation of food proteins. Michaelis‐ Menten kinetics for industrial reactions (mixed zero‐ and first‐ order) were used for predicting the behavior of the reactor and for calculating enzyme dosage required to completely deamidate a given quantity of protein. Using such a reactor in the deamidation of food proteins or protein hydrolysates can lead to new food proteins with superior functional properties from less functional starting materials.