Fractionation and identification of a novel hypocholesterolemic peptide derived from soy protein Alcalase hydrolysates
Fractionation and identification of a novel hypocholesterolemic peptide derived from soy protein Alcalase hydrolysates
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DOI：
10.1016/j.foodres.2007.01.005
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发表时间：
2007-07
影响因子：
8.1
通讯作者：
F. Zhong;Xiaomei Zhang;Jianguo Ma;C. Shoemaker
中科院分区：
文献类型：
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作者：
F. Zhong;Xiaomei Zhang;Jianguo Ma;C. Shoemaker
以大豆蛋白水解液（SAPH DH 18%）为原料，采用大孔吸附树脂（MAR DA 201-C）乙醇梯度洗脱，Sephadex G-15凝胶柱层析和反相高效液相色谱法分离得到一种新的降胆固醇肽。用HPLC-MS鉴定降胆固醇肽的结构。在用MAR DA 201-C进行梯度乙醇洗脱的四个级分中，在75%乙醇级分中发现具有最高降胆固醇活性的肽。通过每个乙醇洗脱级分的氨基酸组成计算的平均疏水性表明，可以用MAR DA 201-C在疏水性方面分离肽。Sephadex G-15柱层析分离得到4个峰，其中峰2的胆固醇胶束溶解抑制率最高，为81.3%，对应的分子量为300- 800 Da。反相高效液相色谱分离得到15个主峰，峰7的胆固醇胶束溶解抑制率最高（94.3%）。经LC-MS和氨基酸组成分析，该肽的氨基酸序列被鉴定为WGAPSL。
A novel hypocholesterolemic peptide was fractionated by gradient ethanol elution from a macroporous adsorption resin (MAR DA201-C), and then separated on Sephadex G-15 and RP-HPLC from a soy protein hydrolysate (SAPH DH 18%). Identification of the hypocholesterolemic peptide structure was accomplished with HPLC–MS. The peptide with the highest hypocholesterolemic activity was found in 75% ethanol fraction among the four fractions from gradient ethanol elution with MAR DA201-C. The calculated average hydrophobicity by amino acid composition of each ethanol eluted fraction suggested that the peptides could be separated in terms of hydrophobicity with MAR DA201-C. Four peaks were obtained with further fractionation on Sephadex G-15, the highest cholesterol micellar solubility inhibition rate, 81.3%, was obtained in Peak 2, corresponding to the molecular weight fraction of 300–800Da. Fifteen main peaks were obtained with RP-HPLC fractionation, the highest cholesterol micellar solubility inhibition rate (94.3%) was in Peak 7. The amino acid sequence of this peptide was identified as WGAPSL with LC–MS and amino acid composition analysis.