Microbial transglutaminase-mediated modification of ovalbumin

In the present paper we have investigated the impact of microbial transglutaminase on thermally treated ovalbumin. In fact, ovalbumin was modified by microbial transglutaminase following heat treatment for 1 h at 80 °C. The protein was both intra- and inter-molecularly crosslinked as shown by the formation of high molecular weight polymers and a monomer having similar molecular weight but higher electrophoretic mobility when compared to unmodified ovalbumin. Analysis of simulated digestion under physiological conditions has demonstrated that the biopolymers obtained after transglutaminase treatment were more resistant to both gastric and duodenal digestion. Whilst they started gradually being digested after 5 min of incubation with pepsin, some of them were still present even after 60 min incubation with the duodenal enzymes, trypsin and chymotrypsin. Furthermore, incubation of 1.5% (w/v) ovalbumin gel in the presence of transglutaminase led to the formation of a well-developed viscoelastic gel network with higher modulus and lower phase angle values. These results suggest a possible use of transglutaminase-modified ovalbumin in the food industry as a potential ingredient to enhance both the functional properties of many food-based products, such as digestibility, and mechanical properties, such as viscoelasticity and gel strength.

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► Ovalbumin is able to act as a substrate of the enzyme Transglutaminase (TG).
► TG modification affects the gastric and duodenal digestion of ovalbumin.
► TG leads to formation of ovalbumin gels with higher elasticity.