Malomo Sunday Abiodun (Publications)
Publisher Journal Of The American Oil Chemists Society
Publication Type Journal
Publication Title In Vitro Acetylcholinesterase-inhibitory Properties Of Hemp Seed Protein Hydrolysates
Publication Authors Malomo, S.A. and Aluko, R.E. 2016.
Year Published 2016

 The aim of this work was to characterize the

structural and functional properties of hemp seed proteinderived

acetylcholinesterase (AChE)-inhibitory enzymatic

hydrolysates. Hemp seed protein isolate hydrolysis was

performed using six different proteases (pepsin, papain,

thermoase, flavourzyme, alcalase and pepsin pancreatin)

at different concentrations (1–4 %). The degree of hydrolysis

was directly related to the amount of protease used but

had no relationship with AChE-inhibitory activity. Amino

acid composition results showed that the hemp seed protein

hydrolysates (HPHs) had high levels of negatively

charged amino acids (39.62–40.18 %) as well as arginine.

The 1 % pepsin HPH was the most active AChE inhibitor

with ~6 μg/mL IC50  value when compared to 8–11.6 μg/mL

for the other HPHs. Mass spectrometry analysis showed

that most of the peptides in all the hydrolysates were less

than 1000 Da in size. However, the pepsin HPHs contained

larger-sized peptides (244–1009 Da) than the papain HPHs

(246–758 Da), which in turn was larger than the alcalase

HPH (246–607 Da). The higher AChE-inhibitory effects

of the pepsin HPHs may be due to increased synergistic

effects from a wider peptide size range when compared to

the papain and alcalase HPHs that had narrower ranges.

The narrow peptide size range in the alcalase HPH confirms

the higher efficiency of this protease in releasing

small-sized peptides from food proteins.