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Antioxidant activities and emulsifying properties of porcine plasma protein hydrolysates modified by oxidized tannic acid and oxidized chlorogenic acid

Yichun Chen, Shuai Jiang, Qian Chen, Qian Liu, Baohua Kong
Process biochemistry 2019 v.79 pp. 105-113
Fourier transform infrared spectroscopy, antioxidant activity, antioxidants, blood proteins, chlorogenic acid, crosslinking, emulsifiers, emulsifying, emulsifying properties, hydrogen bonding, hydrophobicity, oxidation, protein hydrolysates, swine, tannins, turbidity
Physicochemical characteristics, antioxidant activities and emulsifying properties of porcine plasma protein hydrolysates (PPPH) modified with oxidized tannic acid (OTA) or oxidized chlorogenic acid (OCA) were investigated. The formation of complexes was showed by increased turbidity, and both OTA and OCA were covalently attached to PPPH as shown by the significantly decrease in free amino group contents (P < 0.05). Fourier transform infrared spectroscopy also indicated cross-linking between PPPH and OTA or OCA through hydrogen bonds. More importantly, compared with PPPH alone, modification of OTA or OCA endowed PPPH with a higher emulsifying stability index and greater antioxidant activities. However, the emulsifying activity index of PPPH significantly decreased after modification (P < 0.05), which is associated with lower surface hydrophobicity. These results suggest that PPPH-OTA and PPPH-OCA complexes could be used as efficient antioxidants and potential emulsifiers in emulsion-food systems.