Unlocking the functional potential of porcine hemoglobin: An enzymatic hydrolysis-phosphorylation synergistic modification to enhance minced pork quality

Abstract

The impact of enzymatic hydrolysis-phosphorylation synergistic modification on the functional properties and structural alterations of porcine hemoglobin (PHb) were investigated, and the impact of the modified protein on the quality of minced pork was explored. The results indicated that, compared to PHb, the surface hydrophobicity of hydrolyzed-phosphorylated porcine hemoglobin (HP-PHb) was reduced, and its solubility and emulsification properties were significantly enhanced. Moreover, HP-PHb exhibited the highest DPPH radical scavenging, the strongest hydroxyl radical scavenging activity, the highest ABTS cation radical scavenging ability and Fe²⁺ chelating ability. The SDS-PAGE results indicated that enzymatic hydrolysis led to the degradation of PHb, resulting in the generation of more small peptides, while phosphorylation modifications did not alter the overall structure of the protein. Thermal analysis demonstrated that HP-PHb had a higher thermal stability. Scanning electron microscopy images revealed a looser structure with the appearance of smaller particles. These findings illustrated that synergistic modification significantly enhances the properties of HP-PHb, which is beneficial for efficient utilization in food processing. The addition of HP-PHb improved the pH and water retention of minced pork, reducing the cooking loss from 38 % to 34 %. The non-mobile water peak surface area increased, indicating enhanced water retention. Additionally, HP-PHb contributed to better structural properties, resulting in greater elasticity and a denser fibrous structure in the minced pork. This study provides new insights into protein modification, aiming to increase the added value of porcine blood and its extensive application in meat products.