| Literature DB >> 33051101 |
Tong Shi1, Hui Liu1, Teng Song1, Zhiyu Xiong1, Li Yuan1, David Julian McClements2, Wengang Jin3, Quancai Sun1, Ruichang Gao4.
Abstract
The effects of l-arginine (Arg)-assisted ultrasonic treatment on the molecular and interfacial characteristics of myosin and emulsifying properties of the emulsion were evaluated to ascertain the underlying mechanism in improving the emulsion stability. Ultrasonication induced the exposure of residues of native myosin, which was increased by the addition of Arg (40 mM). Furthermore, in terms of emulsions containing Arg, the higher the ultrasonication intensity was, the greater the increase in adsorbed protein (from 15.43 ± 0.28% to 50.49 ± 1.65%) and π value, and the decrease in droplet sizes (from 4098 nm to 2324 nm) (P < 0.05). Moreover, the increase in the ordered structures of interfacial myosin induced by Arg and ultrasonication favoured the formation of a protein gelation network. In summary, Arg-assisted ultrasonic treatment improved the stability of the emulsion by inducing the exposure of native myosin and facilitating the formation of ordered structures of interfacial myosin.Entities:
Keywords: Arg; Aromatic and aliphatic amino acid residues; Emulsion; Protein gelation network; Stability; Ultrasonication
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Year: 2020 PMID: 33051101 DOI: 10.1016/j.foodchem.2020.128314
Source DB: PubMed Journal: Food Chem ISSN: 0308-8146 Impact factor: 7.514