期刊
INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY
卷 57, 期 4, 页码 2556-2567出版社
WILEY
DOI: 10.1111/ijfs.15630
关键词
gel properties; l-histidine; l-lysine; myofibrillar proteins; oxidative characteristics
资金
- Yangzhou University Science and Technology Innovation Projects [137012527]
This study investigated the effects of l-lysine and l-histidine on the oxidative characteristics and gel properties of porcine myofibrillar proteins. The results showed that lysine and histidine had strong iron-chelating ability and hydroxyl radical scavenging activity. Additionally, they inhibited protein carbonyl formation and protein aggregation in a dose-dependent manner. Furthermore, lysine and histidine improved the water-holding capacity and gel strength of the protein gels, resulting in better gel quality.
This study investigated the effects of l-lysine (Lys) and l-histidine (His) on the oxidative characteristics and gel properties of porcine myofibrillar proteins (MP). Results showed that Lys and His had a strong ferrous ion-chelating ability and hydroxyl radical-scavenging activity. Moreover, Lys and His inhibited the protein carbonyl formation and MP aggregation at 0.2 M and 0.6 M NaCl, respectively, in a dose-dependent manner. Furthermore, 2 and 4 mg mL(-1) Lys and His decreased the oxidation-induced loss of the tertiary structure of MP accompanied by the lower surface hydrophobicity. The water-holding capacity and gel strength of MP gels increased with increasing Lys and His concentrations due to more regular and lamellar structures with smaller and homogeneous pores at 0.6 M NaCl and more orderly crosslinking via fibrous filament at 0.2 M NaCl. In summary, Lys and His chelated the ferrous ions and scavenged hydroxyl radicals, decreased the oxidation-induced physicochemical changes, thus preventing oxidative damage during the formation of a three-dimensional gel network, which resulted in better gel quality.
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