Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 403-410 |
| Number of pages | 8 |
| Journal | Food Chemistry |
| Volume | 118 |
| Issue number | 2 |
| DOIs | |
| State | Published - Jan 15 2010 |
Bibliographical note
Funding Information:This study was supported by foundation of Science and Technology of 11th Five-year Plan of Heilongjiang (Grant No. GB06B403).
Keywords
- Antioxidant peptide
- Functional properties
- Porcine plasma protein hydrolysate
- Purification
ASJC Scopus subject areas
- Analytical Chemistry
- Food Science