AI Article Synopsis
- A study analyzed swim bladder polypeptides (SBPs) for their antioxidant properties and found that optimal conditions for enzyme treatment included an alkaline protease with specific ratios, time, and temperature.
- Three molecular weight fractions were created, with F3 demonstrating the highest antioxidant activity, effectively removing reactive oxygen species like O•, DPPH•, and •OH.
- F3 also contained beneficial amino acids and was shown to inhibit enzymes linked to hypertension, making it a promising source of bioactive peptides.
Article Abstract
Swim bladder polypeptides (SBPs) of were analyzed for their antioxidant activity and physicochemical properties. The results showed the optimal enzymatic conditions were alkaline protease with a solid-to-liquid ratio of 1:20, an incubation time of 4 h, a temperature of 55 °C, and an enzyme dosage of 5000 U/g. Three different molecular weight fractions (F1, F2, and F3) were obtained via ultrafiltration. F3 (912.44-2135.82 Da) showed 77.90%, 72.15%, and 66.25% removal of O•, DPPH•, and •OH, respectively, at 10 mg/mL, which was significantly higher than the F1 and F2 fractions ( < 0.05). F3 contained proline (6.17%), hydroxyproline (5.28%), and hydrophobic amino acids (51.39%). The UV spectrum of F3 showed maximum absorption at 224 nm. Peptide sequence analysis showed that F3 contained antioxidant peptides (MFGF, GPPGPRGPPGL, and GPGPSGERGPPGPM) and exhibited inhibitory activities on angiotensin-converting enzyme and dipeptidyl peptidase III/IV (FRF, FPFL and LPGLF). F3 was considered a good raw material for obtaining bioactive peptides.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10217141 | PMC |
| http://dx.doi.org/10.3390/foods12101934 | DOI Listing |
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