Preparation and antioxidative properties of a rapeseed ( Brassica napus ) protein hydrolysate and three peptide fractions.
This study investigated the possibility of converting the insoluble rapeseed meal protein into functionally active ingredients for food applications. The rapeseed ( Brassica napus ) meal protein isolates were first digested by Alcalase and Flavourzyme, and the resultant rapeseed crude hydrolysate (RSCH) exhibited a dose-dependent reducing antioxidant power and hydroxyl radical scavenging ability. RSCH could also inhibit the malonyldialdehyde (MDA) generation by 50% in blood serum at 150 mg/mL. RSCH was further separated into three fractions (RSP1, RSP2, and RSP3) by Sephadex gel filtration according to their different molecular weights. The amino acid compositions and antioxidant potentials were assessed for RSP1-3 fractions. All three fractions showed inhibiting effects on superoxide anion generation to various extents. They could also inhibit the autohemolysis of rat red blood cells and MDA formation in rat liver tissue homogenate. The results suggested that rapeseed peptide hydrolysate may be useful as a human food addition as a source of bioactive peptides with antioxidant properties.
Xue
Zhaohui
Z
School of Agriculture and Bioengineering, Tianjin University, Tianjin, Peoples' Republic of China.
Yu
Wancong
W
Liu
Zhiwei
Z
Wu
Moucheng
M
Kou
Xiaohong
X
Wang
Jiehua
J
D000818:Animals; D000975:Antioxidants / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D029741:Brassica rapa / Q000737:chemistry*; D005260:Female; D008297:Male; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D011492:Protein Hydrolysates / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D051381:Rats; D017208:Rats, Wistar
D000975:Antioxidants; D010455:Peptides; D010940:Plant Proteins; D011492:Protein Hydrolysates