Purification, Identification and Evaluation of the Stability of Angiotensin I-converting Enzyme Inhibitory Peptides Derived from By-products of Casein Phosphopeptides
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Abstract:
By-products of casein phosphopeptide contain abundant functional peptides, from which angiotensin I-converting enzyme (ACE-I) inhibitory peptides with antihypertensive activity can be recycled. This is of significance for utilizing waste and protecting the environment. Based on previous research on technology that accumulates bioactive peptides, the peptide monomers with antihypertensive activity were isolated and purified from crude-enriched products, and the molecular weights of peptide monomers, their primary sequences, and stabilities were studied. The results showed that, using the crude products as raw materials, ACE-I inhibitory peptide monomers with high activity, P16 and P18, could be obtained in just two steps, including anion-exchange chromatography and HPLC. The molecular weight of P16 was 742.6 and its primary sequence was GPFPIIV, which was discovered for the first time. The molecular weight of P18 was 1385.8 and its primary sequence was FFVAPFPEVFGK. Both P16 and P18 possessed high acid-base resistance and thermal stability. Various degrees of decomposition occurred in both peptides in the in vitro gastrointestinal digestion test. Nevertheless, the activity of P16 increased by 12.8%, while that of P18 decreased by 37.5%. Thus, the rise and decline were related to the exposure or destruction of the active centers.
