Isolation, Purification And Antioxidant Activity Of Defatted Sheep Brain Proteolytic Peptides
Keywords
Sheep Brain Protein, Peptide, Isolation And Purification, Antioxidant Activity
Abstract
In order to prepare antioxidant peptides from sheep brain protein, this experiment analyzed the content and amino acid composition of defatted sheep brain protein; sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was used ) The molecular weight of the enzymatic hydrolyzate of Bacillus subtilis neutral protease at different enzymatic hydrolysis times was analyzed; the enzymatic hydrolysis products of sheep brain were separated step by step using Sephadex G-25 and Sephadex G-15. After purification, the antioxidant activity of the isolated components was evaluated using the hydroxyl radical (¡¤OH) and nitrite ion scavenging capabilities as indicators, and the antioxidant activity of the purified components was measured. The results showed that the protein content of defatted sheep brain powder was 60.55%. Among the 17 amino acids measured, the two acidic amino acids glutamic acid and aspartic acid had the highest content and contained 7 essential amino acids; sheep brain protein was enzymatically After solution, the molecular mass was concentrated below 10 kD; after purification by Sephadex G-25, 6 components were obtained, of which component F4 had the strongest antioxidant activity. After component F4 was purified by SephadexG-15, 3 components were obtained Components, among which component F4-2 has the strongest antioxidant activity, and component F4-2 has the strongest antioxidant activity against 1,1-diphenyl-2-trinitrophenylhydrazyl (DPPH) The half inhibition rates IC50 of free radicals, ¡¤OH, superoxide anion radicals (O2-¡¤), and nitrite ions are 1.64, 2.47, 7.98, and 5.14 mg/mL respectively.
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Original research done by Chang Fei, Yang Xueguo, Duan Xuchang, Xiao Shicheng, Jiang Pengfei, Huang Huina
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