## 4 Summary  
The mussel meat yield and resulting hydrolysate yields showed season-specific trends and this related to the fat and protein content of generated hydrolysates. Mussel meat yields were 9.75% to 21.69%, 0.37% \(\pm\) 0.11% to 0.52% \(\pm\) 0.17%, 36.77% \(\pm\) 7.17% to 52.19% \(\pm\) 3.33% for mussel meat and 3.33% \(\pm\) 0.93% to 7.17% \(\pm\) 0.65%, 0.97% \(\pm\) 0.06% to 2% \(\pm\) 0%, 33.48% \(\pm\) 1.45% to 36.99% \(\pm\) 1.27% for  
Figure 8: AChE enzyme inhibition (%) by inhibition by mussel Protamex® hydrolysates. Nine samples from the three sampling sites, Mulroy bay (MB), Killary harbor (KH) and Ardgyrom (A), collected from November 2018 to October 2019, were used for analysis at a concentration of 1 mg/mL. *The positive control showed significantly higher AChE inhibition as compared to all the samples. Assays were performed in triplicate (n = 3). Figure 9: **(a)** The % ACE-I enzyme inhibition (%) by mussel Protamex® hydrolysates. Six representative unhydrolyzed musse broth samples (MB) and corresponding hydrolysates (H) from the three sampling sites, Mulroy bay (MB), Killary harbor (KH) and Ardgyrom (A), collected from November 2018 to July 2019, were used for analysis at a concentration of 1 mg/mL against captopril (the positive control). **(b)** The IC\({}_{50}\) curve for the Killary harbour November 2018 sample (KHN18). The positive control showed significantly higher ACE inhibition as compared to all the samples and all the hydrolysates showed significantly higher ACE inhibition as compared to unhydrolyzed samples. Assays were performed in triplicate (n = 3). hydrolyses harvested during the period from February to May (during the gamete development season). This is compared to values of 15.34% to 22%, 2.5% \(\pm\) 1.32% to 6.36% \(\pm\) 1.2%, 65.78% \(\pm\) 0.54% to 68.31% \(\pm\) 1.02% for mussel meat and 7.97% \(\pm\) 0.39% to 9.57% \(\pm\) 0.94%, 0.96% \(\pm\) 0.05% to 2% \(\pm\) 0%, 35.57% \(\pm\) 1.02% to 40.54% \(\pm\) 2.12% for hydrolyses generated with July-October samples (during the blue mussel spawning season). All the hydrolyses were rich in essential amino acids, taurine, polyunsaturated fatty acids EPA and DHA, and contained several unique bioactive peptides with ACE-I inhibitory activity. Few hydrolyses had DPP-IV inhibitory activities (AJuly19, KHS19 and KHO19) and hydrolyses generated with these samples also inhibited AChE. The in silico results were in agreement with the results seen through in vitro enzyme inhibition assays. Peptides obtained from the 3-kDa fraction of the hydrolyses were medium-to-large sized, having >7 amino acids. The hydrolyses showed good emulsion activity and excellent protein solubility profiles over a range of pH and can thus be incorporated in further product formulation studies targeting cardiovascular diseases and obesity. The study enabled the characterisation of raw material and hydrolysate products through a sampling period of one year. In future, inhibitory peptides from marine sources need not be limited to over-exploited green lipped mussels. The bio-active-rich composition of the resulting hydrolyses from lesser studied _Mytilus edulis_ mussels opens doors for nutraceutical products. Further, in silico studies can be undertaken using blue mussel-derived sequenced peptides to dock critical enzymes such as prolyl endopeptidase, cyclooxygenase 1 and 2, along with dipeptidyl peptidase, acetylcholinesteraseiesterase and angiotensin-converting enzyme-1. The enzymes have been implicated in several disorders such as mental degeneration, inflammation, diabetes, cardiovascular diseases and other metabolic diseases. Conceptualisation, M.H. ; methodology, A.S.N. ; validation, A.S.N., M.H. ; formal analysis, A.S.N., L.M. ; investigation, M.H. and A.S.N. ; writing--original draft preparation, A.S.N. ; writing--review and editing, A.S.N. and M.H. ; supervision, M.H. ; project administration, M.H. ; funding acquisition, M.H. All authors have read and agreed to the published version of the manuscript.