In vitro ACE-1 inhibitory peptides were characterised previously from a number of microalgal species including (peptide IAPG), (peptides FDL, AFL, VVPPA), (peptide YMGLDLK), (peptides IW and LW) and indeed (peptides GMNNLTP and LEQ). The isolation of protein from 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) IC value for the generated permeate fraction was 370 µg/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 biomass as both a protein and bioactive peptide resource, which could be harnessed for use in the development of functional foods and feeds.