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| Effects of L-Arginine on Emulsifying Properties of Pork Sarcoplasmic Protein |
| WANG Yu, LIU Ningning, WANG Jiale, MENG Shaohua, CHEN Bo, LI Ke, LI Junguang, LI Shengjie, BAI Yanhong |
| 1. Collaborative Innovation Center of Production and Safety, Henan Province, Key Laboratory of Cold Chain Food Processing and Safety Control, Ministry of Education, College of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450001, China; 2. Henan Shuanghui Investment Development Co. Ltd., Luohe 462000, China; 3. School of Food Science and Technology, Dalian Polytechnic University, Dalian 116033, China |
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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.
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2025, Vol. 39 
