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  • Title: Rapid purification and characterization of angiotensin converting enzyme inhibitory peptides from lizard fish protein hydrolysates with magnetic affinity separation.
    Author: Lan X, Liao D, Wu S, Wang F, Sun J, Tong Z.
    Journal: Food Chem; 2015 Sep 01; 182():136-42. PubMed ID: 25842319.
    Abstract:
    In this study, angiotensin converting enzyme (ACE) inhibitory peptides from lizard fish protein hydrolysate with neutral protease were purified through magnetic affinity separation. Magnetic agarose microsphere was prepared by reverse-phase microemulsion method, and its surface was modified with epoxy groups to immobilize ACE as a magnetic affinity medium (MAM-ACE) and then mixed with lizard fish ultrafiltration hydrolysate (<5 kDa). The MAM-ACE was recovered by a magnet. The bound peptides were released by 1M NaCl and further purified by reverse-phase high-performance liquid chromatography. The amino acid sequence of the peptide with the highest ACE inhibitory activity was identified as Gly-Met-Lys-Cys-Ala-Phe, and its IC50 was 45.7 ± 1.1 μM. The result indicates that MAM-ACE is a faster and more efficient method for purifying micro-bioactive peptides from food protein complex mixtures compared with ion exchange and gel chromatography.
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