Research Article | OPEN ACCESS
Physicochemical Changes of Antioxidant Peptides Hydrolyzed From Porcine Plasma Protein Subject to Free Hydroxyl Radical System
1Hehong Yang, 1Yanqing Li, 1Peijun Li, 1Qian Liu, 1Baohua Kong, 2Xu Huang and 3Zengbao Wu
1Department of Food Science, Northeast Agricultural University, Harbin, Heilongjiang, 150030, China
2Department of Gastroenterology, Renmin Hospital of Wuhan University, Wuhan, 430060, China
3Department of Neurosurgery, Renji Hospital of Shanghai Jiao Tong University,
Shanghai, 200127, China
Advance Journal of Food Science and Technology 2013 1:14-18
Received: September 14, 2012 | Accepted: October 24, 2012 | Published: January 15, 2013
Abstract
Antioxidant peptides have attracted much attention for potential application as natural food ingredients but the fate of them, as well as oxidized proteins in foods during processing, is still poorly understood. Physicochemical changes in antioxidant peptides hydrolysated from porcine plasma protein were discussed in a free hydroxyl radical-mediated oxidation system. Porcine Plasma Protein Hydrolysates (PPH) was prepared by hydrolyzing porcine plasma protein with Alcalase for 5 h at pH 8.0, 55°C. The content of carbonyl groups increased significantly at various degrees when PPH exposed to free radical-mediated oxidation for different time and different concentrations of H2O2, while total sulfhydryls, reactive sulfhydryls and free amines contents decreased. It was concluded that PPH played an antioxidant role in the radical-mediated oxidation system. This provides a potential way for antioxidation in food production.
Keywords:
Aantioxidant peptide, free radical-mediated oxidation, physicochemical changes, porcine plasma protein,
Competing interests
The authors have no competing interests.
Open Access Policy
This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
Copyright
The authors have no competing interests.
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ISSN (Online): 2042-4876
ISSN (Print): 2042-4868 |
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