With the implementation of the Outline of “Healthy China 2030” Plan and the continuous enhancement of consumers’ concept of healthy diet, “low salt and phosphorus free” healthy meat products have gradually become a trend of development in the meat products industry. However, simply reducing the addition of NaCl and polyphosphates will seriously affect the cooking yield and quality of the final products. Therefore, it is of great significance to seek green and healthy alternatives to NaCl and polyphosphates. In recent years, the basic amino acids arginine, lysine and histidine have attracted extensive research attention for their application as substitutes for NaCl and polyphosphates in the meat products industry. This paper reviews the latest progress in the study on the regulatory effects of basic amino acids on the structure, solubility, and emulsification and gelation properties of myofibrillar proteins, as well as the underlying mechanisms. Meanwhile, the effects of basic amino acids on meat quality (color, water retention, texture characteristics, and oxidation stability) are also summarized. Hopefully, this review will provide a theoretical basis for the follow-up research and practical application of basic amino acids in the meat industry.

This study was conducted in order to investigate the mechanism of the effect of adding different concentrations of L-lysine (L-Lys) on the gelling properties of porcine myofibrillar protein (MP) damaged by repeated freeze-thaw cycles. The changes in the conformation, solubility and gelling properties were analyzed by means of circular dichroism (CD) spectroscopy, intrinsic tryptophan fluorescence spectroscopy, a rheometer, a texture analyzer and a scanning electron microscope. The results showed that the addition of L-Lys caused an increase in the α-helix content and intrinsic tryptophan fluorescence intensity of freezing-damaged MP. The solubility of freezing-damaged MP gradually increased with increasing L-Lys concentrations, the storage modulus (G’), gel strength, cooking loss and gel whiteness gradually decreased, and the gel microstructure became gradually more uniform. On the whole, the addition of L-Lys significantly reduced the gel strength and cooking loss of repeatedly frozen-thawed MP gel by changing the conformation, and could thus improve the water-holding capacity and tenderness of freezing-damaged meat.

Six phenolic acids (PAs) with related structures, i.e., gallic acid (GA), syringic acid (SA), coumaric acid (CMA), caffeic acid (CFA), ferulic acid (FA), and chlorogenic acid (CA), were compared for their effects on the gelling properties of myofibrillar protein (MP) under oxidative conditions. Of the six PAs, only the smallest GA caused significant reductions of free amine and sulfhydryl content (by 26% and 7%, respectively, P < 0.05) and SA decreased protein carbonyl formation, while CA, the largest PA with an esterified quinic group, prevented oxidative loss of amines. All PAs quenched MP fluorescence with CA showing the highest efficacy (38% suppression). During thermal gelation, the GA-modified MP displayed the strongest myosin cross-linking. The elasticity (G′) and breaking strength of MP gels were markedly enhanced by the addition of PAs, and the final G′ value ranked in the order GA > CA > FA > CMA > SA > CFA, indicating complex roles of phenolic side groups.