Enzymatic cross-linking of casein nanoparticles across the scales: Fundamental mechanisms and technological potentials

© Jaros

Transglutaminase is an enzyme that catalyses the formation of isopeptide bonds between protein bound glutamine and lysine residues and therefore the polymerisation of single protein molecules. In the food sector, transglutaminase of microbial origin (mTGase) is used in the meat and fish industry, for instance for ham and surimi production. Other reported applications refer to milk proteins, as casein represents an excellent substrate for the enzyme.

In a recently completed joint project it was demonstrated that the action of mTGase on casein molecules, which are non-covalently associated to nanoparticles, results in the formation of intra-particle cross-links. This leads to a fixation of the molecules and significant changes in the shape and density of the particles. Cross-linking intensity itself depends on environmental factors, including for example ionic strength of the substrate. The aim of this project it to broaden the range of particle sizes that can be obtained from cross-linking with mTGase by varying additional factors. After fundamental analysis of the molecular and colloidal properties of the differently sized nanoparticles, their application potential will be demonstrated by using two prominent examples. Project hypothesis is that the self-association of non-micellar casein to hydrated nanoparticles, driven by concentration, ionic strength and by temperature, enables us to fixate and modify their conformation and to create differently sized nanoparticles with a great potential for selected applications.

In cooperation with:

Leibniz-Institut für Polymerforschung Dresden e.V., AG Polymerseparation (PD Dr. Albena Lederer)

Supported by:

Deutsche Forschungsgemeinschaft

Project researchers and contact:

© Surber

Name

PD Dr.nat.techn. et Ing.habil Doris Jaros

Product technologies: Milk; Biomacromolecules

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