An angiotensin converting enzyme inhibitory peptide prepared from pig slaughter blood

摘要

A considerable amount of slaughter blood from pork slaughterhouses is currently inferior in its utility value, which makes it difficult to treat wastewater. To prevent environmental pollution such as pollution of water source and to save the cost of wastewater treatment, and to separate antihypertensive peptides, which are old value-added new functional materials, from slaughter blood, The slaughter blood is immediately slaughtered and stored in a storage tank to prevent blood clotting, and then separated into plasma and blood cells through a continuous centrifuge. The low molecular weight peptides present in the supernatant obtained by adding 2% trichloroacetic acid to the separated plasma were fractionated using Sephadex or Biogel gel permeation chromatography, and then the crude angiotensin L-histidine-L-leucine was used as a substrate for the enzyme activity of angiotensin converting enzyme (ACE), and the fraction having a high degree of inhibition was further subjected to reversed phase high pressure liquid chromatography The peptide was separated and purified using a chromatography C ₈ column, and the sequence was confirmed using a peptide sequencer.