@article{WANG2025, 
author = {Yu WANG and Ningning LIU and Jiale WANG and Shaohua MENG and Bo CHEN and Ke LI and Junguang LI and Shengjie LI and Yanhong BAI},
title = {Effects of L-Arginine on Emulsifying Properties of Pork Sarcoplasmic Protein},
year = {2025},
journal = {Meat Research},
volume = {39},
number = {3},
pages = {1-7},
keywords = {structural modification, emulsifying properties, pork, sarcoplasmic protein, L-arginine},
url = {https://www.sciopen.com/article/10.7506/rlyj1001-8123-20240819-213},
doi = {10.7506/rlyj1001-8123-20240819-213},
abstract = {The effects of different mass fractions of L-arginine (0.0%, 0.5%, 1.0%, and 1.5%) on the emulsifying characteristics of pork sarcoplasmic protein were studied. The findings indicated that addition of L-arginine (≥ 1%) significantly enhanced the emulsifying activity and emulsion stability of sarcoplasmic protein (P < 0.05) and decreased the particle size (D4,3, D50, and D90) of sarcoplasmic protein-stabilized emulsion (P < 0.05). The Turbiscan stability index (TSI) decreased after addition of L-arginine. The results of interfacial rheology showed that L-arginine increased the oil-water interfacial tension. The results of surface hydrophobicity and ultraviolet (UV) absorption spectroscopy implied that L-arginine promoted the exposure of protein hydrophobic groups (tryptophan and tyrosine residues). Raman spectroscopy showed that L-arginine was beneficial for the secondary structure transformation of sarcoplasmic protein from α-helix to β-turn. The results of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) showed that the basic composition of sarcoplasmic protein was not affected by L-arginine. In summary, L-arginine could significantly improve the emulsifying properties of sarcoplasmic protein by changing emulsion physicochemical properties, protein interfacial characteristics, and protein secondary and tertiary structures.}
}