【摘要】 对以中国毛虾为原料酶法制备具有抑制血管紧张素转换酶(ACE)活性的酶解产物的方法作了探讨。以体外活性(ACE抑制率)为指标,通过正交试验确定胃蛋白酶的最佳酶解条件为pH2.4、温度41℃、酶量900U·g-1底物、底物浓度8%;酶解产物的IC50为0.65mg·mL-1,再分别利用SephadexG 25和SephadexG 15对其进行进一步分离提纯,IC50降至0.084mg·mL-1和0.046mg·mL-1,活性组分中的疏水性氨基酸含量增高,最终活性产物的分子量分布在700～1900。更多还原

【Abstract】 Preparing angiotensin I-converting enzyme inhibitors derived from the enzymatic hydrolysate of Acetes chinensis was discussed in this paper. To get the optimal conditions of peptic hydrolysis we did orthogonalty trials with the ACE inhibitory ratio in vitro being the index. The hydrolysate with IC₅₀ being 0.65 mg·mL^-1 was gained under the conditions of pH 2.4, temperature 41℃, enzymatic hydrolysis time 3 hours, enzymatic concentration 900 U·g^-1 substrate and substrate concentration 8%. The hydrolysate was filtrated with a Sepahdex G-25 column, the fraction with the highest ACE inhibitory activity was collected and filtrated with a Sephadex G-15 column, and the fraction with the highest activity was collected again, their IC₅₀ were found to be 0.084 mg·mL^-1 and 0.046 mg·mL^-1, respectively. After purification the content of hydrophobic amino acids tended to increase in the amino acids composition. Molecular weight distribution of the highest ACE inhibitory activity fraction of Sephadex G-15 gel chromagraphy was located between 700 and 1900.更多还原