STRUCTURAL-ANALYSIS OF ANTIOXIDATIVE PEPTIDES FROM SOYBEAN BETA-CONGLYCININ
STRUCTURAL-ANALYSIS OF ANTIOXIDATIVE PEPTIDES FROM SOYBEAN BETA-CONGLYCININ
复制标题
DOI：
10.1021/jf00051a004
复制
发表时间：
1995-03-01
影响因子：
6.1
通讯作者：
YAMAUCHI, F
中科院分区：
文献类型：
--
作者：
CHEN, HM;MURAMOTO, K;YAMAUCHI, F
大豆蛋白 β-伴大豆球蛋白（7S 蛋白）的蛋白酶水解可在 pH 7.0 的水系统中产生针对亚油酸过氧化的抗氧化活性。通过尺寸排阻色谱和反相HPLC，从蛋白酶S制备的水解产物中分离出六种抗氧化肽。使用气相蛋白质测序仪和电子喷雾质谱法测定肽的氨基酸序列。这些肽由 5-16 个氨基酸残基组成，包括 N 端位置的疏水性氨基酸、缬氨酸或亮氨酸，以及序列中的脯氨酸、组氨酸或酪氨酸。
Protease hydrolyses of a soybean protein, beta-conglycinin (7S protein), yielded antioxidative activity against the peroxidation of linoleic acid in an aqueous system at pH 7.0. Six antioxidative peptides were isolated from the hydrolysate prepared with protease S by size exclusion chromatography and reversed-phase HPLC. The amino acid sequences of the peptides were determined using a gas-phase protein sequencer and electron spray mass spectrometry. The peptides were composed of 5-16 amino acid residues, including hydrophobic amino acids, valine or leucine, at the N-terminal positions, and proline, histidine, or tyrosine in the sequences.