Effects of lysine and arginine addition combined with high-pressure microfluidization treatment on the structure, solubility, and stability of pork myofibrillar proteins. (30th December 2022)

• Record Type: Journal Article
• Authors: Zhang, Dong; Wu, Zhicheng; Ruan, Jinggang; Wang, Yizhi; Li, Xueyi; Xu, Min; Zhao, Jie; Lin, Hongbin; Liu, Ping; Wang, Zhaoming; Li, Hongjun
• Is Part Of: Lebensmittel-Wissenschaft + Technologie =. Volume 172(2022)
• Publication Date: 2022-12-30
• Subjects: Lysine and arginine -- High-pressure microfluidization treatment -- Myofibrillar proteins -- Solubility -- Stability; Food industry and trade -- Periodicals; Food -- Composition -- Periodicals; Microbiology -- Periodicals; Nutrition -- Periodicals; 664.005
• DOI: 10.1016/j.lwt.2022.114190
• Languages: English
• ISSNs: 0023-6438

Abstract

Abstract: This study aims to investigate the effects of lysine (Lys) and arginine (Arg) addition combined with high-pressure microfluidization (HPM) treatment on the structure, solubility and stability of pork myofibrillar proteins (MPs). Results show that these treatments can lead to the structural unfolding of MPs, decreased particle size, and increased absolute value of zeta potential, thereby strengthening the interaction between MPs and the solution and significantly increasing solubility and stability. In addition, these treatments result in the production of some soluble polymers in MPs. The addition of Lys and Arg combined with HPM treatment can increase the solubility of MPs from 71.82% to 82.89% and from 71.82% to 85.17%, respectively. Besides, the MPs can still maintain high solubility of 70.43% and 71.84% after 5 day at 4 °C under adding Lys and Arg combined with HPM treatment, respectively. Comprehensive consideration, the method of adding Arg combined with HPM treatment can be considered in production to improve the solubility and stability of MPs. Highlights: The combined use of two treatments can improve the solubility of protein. Both manner caused protein structures to unfold, increasing solvent accessibility. Both manner caused the formation of soluble polymers in the protein. The amino acid addition caused the production of non-disulfide dominated polymers.