Precision Fermentation of Recombinant Myofibrillar Proteins for Future Foods

Abstract Myofibrillar proteins, namely, actin and myosin, are responsible for many of the textural attributes of animal-based meat. Precision fermentation (recombinant production of food ingredients) represents an underexplored approach to producing these proteins without the unsustainable practice of animal agriculture. We show that through the solubility-enhancing SUMO peptide tag and precipitation-based purification, we can produce actin via recombinant DNA methods at titers of 326 mg/L E. coli culture. We also show expression and precipitation of a recombinant fragment of the myosin tail, leading to 572 mg/L culture. For both proteins, yields are improved compared to prior studies, without the need for low-yielding laborious purification columns, with final purities of 69–73%. These recombinant actin and myosin proteins showed macro- and microscopic fibrous features similar to meat. When combined with plant-based proteins, chewiness, hardness, and Young’s modulus were improved toward those of animal-based meat. Preliminary cost analyses suggest a less expensive process for producing myofibrillar proteins compared to established methods. Our results reveal a novel scalable approach to making meat-like foods and ingredients through precision fermentation.