Uncovering the rheological properties basis for freeze drying treatment-induced improvement in the solubility of myofibrillar proteins.

Myofibrillar proteins (MPs) are an important nutritional supplement and have great significance in sports training and rehabilitation therapy. Currently, MPs preservation is still disputed since they are vulnerable to degradation, polymerization, and denaturation. Freeze-drying is an emerging technology for protein preservation, its effects on the functionality of MPs from different sources have not yet been thoroughly studied. This study aims to evaluate the performance differences of freeze-drying in maintaining the functional characteristics of MPs from fish and mammalian sources, providing valuable insights for the processing and preservation of MPs, and providing nutritional support for nursing and rehabilitation. The results showed that freeze-drying was an efficient method for protein preservation, and the effects of freeze-drying on both fish and mammalian sources MPs were significant ( < 0.05) consistent. Specifically, whether before and after freeze-drying, the solubility of fish MPs (FMPs) was significant ( < 0.05) lower than that of mammalian MPs, while the foaming and emulsifying properties were significant ( < 0.05) higher than those of beef and sheep MPs (BMPs and SMPs, respectively). Furthermore, the most efficient protein concentration for freeze-drying was 10 mg/mL, and with this concentration, the gel strengths of BMPs and SMPs showed an insignificant difference ( > 0.05) after freeze-drying.