Related Experiment Video
Updated: Jun 22, 2026

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
Engineering of caseins and modulation of their structures and interactions
Jean-Charles Gaudin1, Annabelle Le Parc1, Benoit Castrec1
1UR 1268 Biopolymères Interactions Assemblages, INRA, 44300 Nantes, France.
Abstract:
Beta-casein (beta-CN) is a milk protein widely used in food industries because of its mild emulsifying properties due to its amphiphilicity. However, the elements determining its micellization behavior in solution and interfacial behavior at the air-water interface are not well known. In order to study how the forced dimerisation influences functional properties of beta-CN, recombinant wild-type beta-CN was produced and distal cysteinylated forms of recombinant beta-CN were engineered. We show that 1) cysteinylated beta-CN formed mainly dimers bridged by disulfide bonds; 2) the process of dimerization adds to the micellization process with temperature and is poorly reversible; 3) covalent disulfide linkage forms at the air-water interface at a lower temperature than in bulk. In conclusion, the location of the cysteinylation in the C-terminus or N-terminus or both is of importance for the properties of beta-CN.
Related Concept Videos
Bacterial Protein Maturation
Production of Pharmaceuticals
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Allosteric Proteins-ATCase
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Microbes in Food Production

