Premium
The in vitro antioxidant properties of alcalase hydrolysate prepared from silkie fowl ( Gallus gallus ) blood protein
Author(s) -
Cheng FuYuan,
Lai IChun,
Lin LiangChuan,
Sakata Ryoichi
Publication year - 2016
Publication title -
animal science journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.606
H-Index - 38
eISSN - 1740-0929
pISSN - 1344-3941
DOI - 10.1111/asj.12509
Subject(s) - hydrolysate , chemistry , antioxidant , dpph , hydrolysis , peptide , biochemistry , lipid peroxidation , food science , enzymatic hydrolysis , chromatography
Two types of proteins including blood plasma protein and blood cell protein were isolated from silkie fowl (Gallus gallus) blood and hydrolyzed using alcalase for 0, 2, 4 and 6 h. The blood plasma protein hydrolysate (BPH) and blood cell protein hydrolysate (BCH) were analyzed for pH value, peptide content and antioxidative properties. The significantly higher peptide contents were observed in BPH than that of BCH, which showed that blood plasma protein was more suitable to hydrolysis by alcalase than blood cell protein. Both BPH and BCH showed strong 2,2‐diphenyl‐1‐picrylhydrazyl (DPPH) radical‐scavenging activity and Fe 2+ chelating ability. BPH at 4 h of hydrolysis (BPH4) demonstrated significantly higher antioxidant capacity than those treated by alcalase in most of the assays. The BPH4 was separated using ultra‐filtration and assessment of the fractions and indicated that low molecular weight of peptides (< 3 kDa) possessed greater DPPH scavenging activity, Fe 2+ chelating ability and inhibitory activity of lipid peroxidation. These results show that BPH has the potential to be ingredients in the food industry as a replacement of synthetic antioxidants.