Antioxidant activity and functional properties of porcine plasma protein hydrolysate as influenced by the degree of hydrolysis

作者：Liu, Qian; Kong, Baohua^*; Xiong, Youling L.; Xia, Xiufang

来源：Food Chemistry, 2010, 118(2): 403-410.

DOI：10.1016/j.foodchem.2009.05.013

• Functional properties
• Purification
• Antioxidant peptide
• Porcine plasma protein hydrolysate

Antioxidant activity and functional properties of porcine blood plasma protein hydrolysates (PPH) prepared with Alcalase at 6.2%, 12.7% and 17.6% of degree of hydrolysis (DH) were investigated. The PPH showed stronger radical-scavenging ability and possessed stronger Cu2+-chelation ability and a reducing power compared to non-hydrolysed plasma protein (P < 0.05). The antioxidant activity of PPH, indicated by thiobarbituric acid-reactive substance (TBARS) values in a liposome-oxidising system, increased with increasing DH (P < 0.05). The Alcalase hydrolysis increased protein solubility from its original 68.46-81.79% (non-hydrolysed) to 82.95-94.94% (hydrolysed) over a broad pH range (3.0-8.0). However, hydrolysis decreased surface hydrophobicity and suppressed emulsifying and foaming capacity of the plasma protein. To identify antioxidant peptide, PPH was subjected to ultrafiltration, ion-exchange chromatography and reverse-phase high performance liquid chromatography (RP-HPLC) and the amino acid sequences of isolated peptides were determined by liquid chromatography/tendem mass spectrometry (LC-MS/MS). The peptide with the strongest antioxidant activity had the amino acid sequence of His-Asn-Gly-Asn. The results indicated that PPH could be used as a novel antioxidant but may be of limited utility as an emulsifying or foaming agent.

• 出版日期2010-1-15
• 单位东北农业大学