河蚌酶解降血压肽的初步分离及性质研究

Separation and Character of Anti-hypertensive Peptides Enzymatically Hydrolyzed from Mussel

以酶解河蚌多肽为原料,对其中的降血压肽进行初步分离及性质研究。采用凝胶Sephadex G-50对河蚌酶解多肽进行分离纯化,得到2个组分MPP1和MPP2,其分子质量分别为14125Da和1271Da。用高效液相色谱(HPLC)测定血管紧张素转化酶(ACE)抑制率,其半抑制浓度(IC50)分别为0.88mg/mL和0.32mg/mL。其中,组分MPP2具有明显的降血压作用。对氨基酸组成的分析表明,MPP2中谷氨酸(Glu)含量最高,即14.04g/100g;疏水性氨基酸含量高达29.76g/100g,与其较高的降血压活性密切相关。

The preliminary separation and characterization of anti-hypertensive peptide （s）, enzymatically hydmlyzed from mussel proteins, were investigated. The fractions of MPP1 and MPP2 were obtained by gel chromatography on column of Sephadex G-50, with the molecular weight distribution of about 14 125 Da and 1 271 Da respectively. The IC50 of angiotensin converting enzyme were 0.88 mg/mL and 0.32 mg/mL respectively analysed by HPLC. The results showed that MPP2 had stronger anti-hypertension effect than that of MPP1. Furthermore, the amino acid composition analysis manifested that the content of Glu in MPP2 was the highest （14.04 g/100 g） and the total content of hydrophobic amino acids was 29.76 g/100 g. This was closely related with the higher anti-hypertension effect.