Purification and Identification of Cholesterol Micelle Formation Inhibitory Peptides of Hydrolysate from High Hydrostatic Pressure-Assisted Protease Hydrolysis of Fermented Seabass Byproduct
| Autor: | Chia-Hua Lin, Guan-Wen Chen, Hong-Ting Victor Lin, Yu-Hsin Lin, Li-Wen Huang |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
0301 basic medicine
Protein Hydrolysates medicine.medical_treatment Hydrostatic pressure Peptide Angiotensin-Converting Enzyme Inhibitors cholesterol micellar solubility hypocholesterolemic peptide Micelle Antioxidants chemistry.chemical_compound Biology (General) Spectroscopy Micelles chemistry.chemical_classification Anticholesteremic Agents Hydrolysis 04 agricultural and veterinary sciences General Medicine 040401 food science Computer Science Applications Lactic acid Chemistry Cholesterol Oligopeptides QH301-705.5 Catalysis Hydrolysate Article Inorganic Chemistry 03 medical and health sciences 0404 agricultural biotechnology medicine Hydrostatic Pressure Animals Amino Acid Sequence Physical and Theoretical Chemistry Molecular Biology QD1-999 030109 nutrition & dietetics Protease Chromatography Organic Chemistry Proteins Molecular Weight high hydrostatic pressure assisted protease hydrolysis chemistry Fermentation Proteolysis Bass Peptides bile acid binding capacity seabass byproduct Peptide Hydrolases |
| Zdroj: | International Journal of Molecular Sciences, Vol 22, Iss 5295, p 5295 (2021) International Journal of Molecular Sciences Volume 22 Issue 10 |
| ISSN: | 1661-6596 1422-0067 |
| Popis: | This research focuses on the proteolytic capacity of sea bass byproduct (SB) and their hypocholesterolemic activity via the cholesterol micelle formation (CMF) inhibition. SB was fermented with seven mixed lactic acid bacteria for 5 h at 42 °C. The lactic fermented SB was hydrolyzed with Protease N for 6 h under HHP to obtain the SB hydrolysates (HHP-assisted Protease N hydrolysis after fermentation, F-HHP-PN6). The supernatant was separated from the SB hydrolysate and freeze-dried. As the hydrolysis time extended to 6 h, soluble protein content increased from 187.1 to 565.8 mg/g, and peptide content increased from 112.8 to 421.9 mg/g, while inhibition of CMF increased from 75.0% to 88.4%. Decreasing the CMF inhibitory activity from 88.4% to 42.1% by simulated gastrointestinal digestion (FHHP-PN6 was further hydrolyzed by gastrointestinal enzymes, F-HHP-PN6-PP) reduced the CMF inhibitory activity of F-HHP-PN6. Using gel filtration chromatography, the F-HHP-PN6-PP was fractioned into six fractions. The molecular weight of the fifth fraction from F-HHP-PN6-PP was between 340 and 290 Da, and the highest inhibitory efficiency ratio (IER) on CMF was 238.9%/mg/mL. Further purification and identification of new peptides with CMF inhibitory activity presented the peptide sequences in Ser-Ala-Gln, Pro-Trp, and Val-Gly-Gly-Thr the IERs were 361.7, 3230.0, and 302.9%/mg/mL, respectively. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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