0571274 - ÚCHP 2024 RIV CH eng J - Článek v odborném periodiku
Hayes, M. - Mora, L. - Lucáková, Simona
Identification of Bioactive Peptides from Nannochloropsis oculata Using a Combination of Enzymatic Treatment, in Silico Analysis and Chemical Synthesis.
Biomolecules. Roč. 12, č. 12 (2022), č. článku 1806. E-ISSN 2218-273X
Grant ostatní: IDEA(XE) NWE 639
Institucionální podpora: RVO:67985858
Klíčová slova: microalgae * protein hydrolysates * pro-peptides
Obor OECD: Industrial biotechnology
Impakt faktor: 5.5, rok: 2022
Způsob publikování: Open access
https://www.mdpi.com/2218-273X/12/12/1806

In vitro ACE-1 inhibitory peptides were characterised previously from a number of microalgal species including Spirulina platensis (peptide IAPG), Chlorella vulgaris (peptides FDL, AFL, VVPPA), Isochrysis galbana (peptide YMGLDLK), Chlorella sorokiniana (peptides IW and LW) and indeed Nannochloropsis oculata (peptides GMNNLTP and LEQ). The isolation of protein from Nannochloropsis oculata using a combination of ammonium salt precipitation and xylanase treatment of resulting biomass combined with molecular weight cut off filtration to produce a permeate and characterisation of bioactive peptides is described. The Angiotensin-1-converting enzyme (ACE-1) IC50 value for the generated permeate fraction was 370 mu g/mL. Ninety-five peptide sequences within the permeate fraction were determined using mass spectrometry and eight peptides were selected for chemical synthesis based on in silico analysis. Synthesized peptides were novel based on a search of the literature and relevant databases. In silico, simulated gastrointestinal digestion identified further peptides with bioactivities including ACE-1 inhibitory peptides and peptides with antithrombotic and calcium/calmodulin-dependent kinase II (CAMKII) inhibition. This work highlights the potential of Nannochloropsis oculata biomass as both a protein and bioactive peptide resource, which could be harnessed for use in the development of functional foods and feeds.
Trvalý link: https://hdl.handle.net/11104/0342535