2025 AOCS Annual Meeting & Expo.
Biotechnology
Sarah G. Corwin, PhD, LDN
Associate Director, Research & Innovation
Ajinomoto Health and Nutrition North America Inc.
Itasca, IL, United States
Transglutaminase (TG) is a natural enzyme which catalyzes the formation of covalent bonds between glutamine and lysine residues, and has a long history of use in meat and seafood binding. More recently, TG has shown utility in non-meat applications, due to its ability to create thermostable food gels with increased water binding. For example, in feta and cheddar cheese, a positive increase in yield due to moisture retention has been observed. Melt restriction results from inter- and intra- molecular bond formation by transglutaminase, which is beneficial in non-melting applications such as cold snacking cheese. In other food gels, such as the binding phase of plant-based meats, transglutaminase can serve as a powerful binder to create the desired bond and chew without undesirable thermoreversible characteristics.