Enhancing the gelation of β-lactoglobulin

The gelation characteristics of bovine β-lactoglobulin A (BLGA) have been enhanced by the selective introduction of cysteine substitutions to increase the free thiol content of the protein. A recombinant version of bovine β-lactoglobulin A (rBLG) has been modified by creating R40C (substitution of arginine at position 40 with cysteine), F82C (substitution of phenylalanine at position 82 with cysteine), and the double R40C/F82C variants. As expected, the number of free thiols increased correspondingly, suggesting that additional disulfide linkages are not formed. The strength of gels formed by heating at 70-90 o C was measured using a microscale penetration test