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β-lactoglobulin a new whey: Computational redesign improves stability and nutritional composition

Researchers redesigned β-lactoglobulin to improve heat tolerance, production yield and branched-chain amino acid content, showing how computational methods may alter food protein performance and nutrition. ProteinMPNN changed up to 20% of the sequence, while PyRosetta identified sites for replacing as many as ten residues. Tests found variants retained similar secondary structures and oligomeric states. ProteinMPNN designs raised titres and thermal stability by up to 15°C. Enriched versions showed altered acid solubility. Surface hydrophobicity had some predictive value for yield. Broader predictive value remains unproven.

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