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ABSTRACT
Globefish (Fugu rubripes) bone collagen (GBC) was isolated and characterized. Electrophoresis and Fourier transform infrared (FTIR) spectra indicated that GBC was high-purity type I collagen with an intact triple-helical structure. Amino acid analysis revealed that GBC contained higher glycine content (364 residues/1,000 residues) than that of other fishery bones, and the imino acid content was 189 residues/1,000 residues. The denaturation temperature (Td) of GBC was 27.1°C. GBC displayed a rapid fibril-forming rate and well-defined fibril morphology in vitro. Globefish bone collagen hydrolysates (GBCH) were optimized by neutral protease through response surface methodology (RSM) with the highest hydroxyl radical (•OH) scavenging capacity. The optimal hydrolysis condition was a reaction temperature of 48.4°C, time of 120 min, and enzyme/substrate ratio of 2520 U/g. Three fractions were collected by ultrafiltration, and the fraction GBCH-III (Mw<1 kDa) possessed the strongest •OH scavenging ability. Reactive oxygen species (ROS) scavenging capacities were evaluated with two model systems: •OH and nitric oxide (NO•). The ROS scavenging capacities increased in a dose-dependent manner. GBCH-III proved to be a more effective •OH scavenger than reduced glutathione (GSH). These findings demonstrated that GBC and GBCH have potential as an alternative source of collagen-derived materials for use in pharmaceutical, nutraceutical, and cosmetic industries.
Funding
The study was supported by the National Science Technology Support Plan Projects (2015BAD17B01) and Qingdao Postdoctoral Application Research Project.