Abstract
Collagen isolated from the ribbon jellyfish (Chrysaora sp.) was hydrolysed using three different proteases (i.e. trypsin, alcalase and Protamex) to obtain bioactive peptides. Angiotensin-I-converting enzyme (ACE) inhibitory activity and antioxidant activities (i.e. ferric reducing antioxidant power (FRAP) and 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity) of the peptides were measured and compared, and the effect of the duration of hydrolysis on the bioactivity (ACE inhibitory and antioxidant activities) of peptides was also evaluated. FRAP activity was the highest in Protamex-induced (25-27 mM) and trypsin-induced hydrolysates (24-26 mM) at 7 and 9 h, respectively. Conversely, hydrolysates produced by trypsin for 1 and 3 h showed the highest DPPH radical scavenging activities (94 and 92%, respectively). Trypsin-induced hydrolysates (at 3 h) also showed the highest ACE inhibitory activity (89%). The peptide sequences with the highest activities were identified using tandem mass spectrometry, and the results show that the hydrolysates had a high content of hydrophobic amino acids as well as unique amino acid sequences, which likely contribute to their biological activities.
Highlights
Hypertension is one of the most common lifestyle-related diseases and has become one of the most significant health problems in recent years [1]
The peptide sequences with the highest activities were identified using tandem mass spectrometry, and the results show that the hydrolysates had a high content of hydrophobic amino acids as well as unique amino acid sequences, which likely contribute to their biological activities
degree of hydrolysis (DH) is an important factor affecting the bioactivity of protein hydrolysates because it influences the size of peptides and the exposure of certain amino acids or functional groups at the peptide terminals [26]
Summary
Hypertension is one of the most common lifestyle-related diseases and has become one of the most significant health problems in recent years [1]. Angiotensin-I-converting enzyme (ACE; EC 3.4.15.1) is a circulating enzyme that plays an important physiological role in regulating blood pressure by converting angiotensin I (inactive form) to angiotensin II, which is a potential vasoconstrictor, or by inactivating bradykinin, which is a vasodilator [2,3,4,5]. Inhibition of ACE can be used to suppress blood pressure elevation and to treat myocardial infarction and other cardio-related diseases [2,4]. Free radicals are the product of normal aerobic reactions in organisms and they play anti-infection roles. If their levels exceed normal levels, they can cause diseases such as cancer, arthritis, atherosclerosis, and diabetes [2]. Neutralizing radicals both in foods and in the body can be helpful in the prevention and treatment of diseases
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