金华火腿中生物活性肽的血管紧张素转化酶调节功能及其分离纯化

Angiotensin-converting Enzyme Regulatory Function of Bioactive Peptides in Jinhua Dry-cured Ham and Its Isolation and Purification

为了探究干腌火腿中生物活性肽的降血压功能,以金华火腿为原料,提取其生物活性肽成分,并通过分离纯化鉴定具有血管紧张素转化酶(ACE)调节功能的生物活性肽。结果表明:经Sephadex G-25分子排阻色谱分离后,金华火腿生物活性肽可分为A、B、C、D共4个组分,其中组分C的ACE抑制活性最强,达到31.8%。将组分C经离子交换柱分离后,金华火腿多肽可分为C1、C2、C3、C4共4个组分,其中C2组分的ACE抑制活性显著高于其它组分,活性高达49.0%(P<0.05)。经Nano-LC-ESI-MS/MS鉴定得到C2中含有8条多肽,经ACE活性测定,序列IESDLERAEE在8条多肽中活性最强,ACE抑制活性达到59.1%。结论:金华火腿多肽具有良好的体外调节ACE活性的功能,为进一步开展其体内血压调节功能研究奠定了基础。

In order to investigate the hypotensive function of bioactive peptides in Jinhua dry-cured ham,the bioactive peptide components were extracted from Jinhua dry-cured ham,and the bioactive peptides with angiotensin-converting enzyme(ACE)modulating function were identified by isolation and purification.The results showed that after separation by Sephadex G-25 molecular exclusion chromatography,the bioactive peptides of Jinhua dry-cured ham could be divided into four fractions,A,B,C and D.Among them,the ACE inhibitory activity of fraction C was the strongest,reaching 31.8%.After fraction C separation by ion exchange column,the Jinhua dry-cured ham peptides could be divided into four fractions,C1,C2,C3 and C4,among which the ACE inhibitory activity of fraction C2 was significantly higher than other fractions,with an activity as high as 49.0%(P<0.05).Eight peptides were identified in C2 by Nano-LC-ESI-MS/MS,and the sequence IESDLERAEE had the highest activity with an ACE inhibitory activity of 59.1%.Conclusion:Peptides derived from Jinhua dry-cured have had good effect of regulating ACE activity in vitro,which lay the foundation for further research on its blood pressure regulation function in vivo.