Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2022 Nov;46(11):e14289.
doi: 10.1111/jfbc.14289. Epub 2022 Jun 27.

Acetylcholinesterase and butyrylcholinesterase inhibitory activities of antioxidant peptides obtained from enzymatic pea protein hydrolysates and their ultrafiltration peptide fractions

Nancy D Asen  1 , Rotimi E Aluko  1   2
Affiliations

Acetylcholinesterase and butyrylcholinesterase inhibitory activities of antioxidant peptides obtained from enzymatic pea protein hydrolysates and their ultrafiltration peptide fractions

Nancy D Asen et al. J Food Biochem. 2022 Nov.

Abstract

This study optimized the enzymatic hydrolysis of yellow field pea proteins using alcalase (ACH), chymotrypsin (CHH), flavourzyme (FZH), pancreatin (PCH), pepsin (PEH), and trypsin (TPH) to obtain hydrolysates and ultrafiltered fractions (<1, 1-3, 3-5 and 5-10 kDa) that possess antioxidant plus acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) inhibitory activities. The hydrolysates exhibited varying degrees of radical scavenging and inhibition of linoleic acid peroxidation, as well as cholinesterase inhibition activities but the potency generally improved by >10% after UF separation into peptide fractions. ACH, FZH, and PEH exhibited significantly (p < .05) higher (20%-30% increases) radical scavenging activities than the other hydrolysates. The 1 and 3 kDa UF fractions of ACH, FZH, and PEH inhibited ~20%-30% AChE activity, while ACH, PCH, TPH, and PEH inhibited ~20%-40% BuChE activity. We conclude that the pea protein hydrolysates and their peptide fractions possess multifunctional properties with potential use against neurodegenerative disorders. PRACTICAL APPLICATIONS: Alzheimer's disease (AD) has multiple pathological pathways in addition to the loss of acetylcholine (ACh) catalyzed by acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE). The presence of severe oxidative stress triggered by lipid peroxidation and formation of free radicals is a common trait in AD patients. The concept of AChE and BuChE inhibition as an approach toward AD amelioration involves the use of compounds with a similar structure to ACh, the natural substrate. Peptides derived from food proteins consist of ester bonds with structural similarity to ACh and theoretically possess the ability to interact with AChE and BuChE. Results from the present study imply that pea protein-derived peptides are potential candidates for use as inhibitors of AChE and BuChE activities, with application in the prevention and management of AD.

Keywords: Alzheimer's disease; acetylcholinesterase; antioxidant; butyrylcholinesterase; enzyme inhibition; membrane ultrafiltration; protein hydrolysates.

PubMed Disclaimer

References

REFERENCES

    1. Acharya, J., Dutta, M., Chaudhury, K., & De, B. (2018). Metabolomics and chemometric study for identification of acetylcholinesterase inhibitor(s) from the flower extracts of Nymphaea pubescens. Journal of Food Biochemistry, 42(5), e12575.
    1. Aderinola, T. A., Alashi, A. M., Nwachukwu, I. D., Fagbemi, T. N., Enujiugha, V. N., & Aluko, R. E. (2020). In vitro digestibility, structural and functional properties of Moringa oleifera seed proteins. Food Hydrocolloid, 101, 105574.
    1. Ahammed, S., Afrin, R., Uddin, N., Al-Amin, Y., Hasan, K., Haque, U., Islam, K. M. M., Alam, A. H. M. K., Tanaka, T., & Sadik, G. (2021). Acetylcholinesterase inhibitory and antioxidant activity of the compounds isolated from Vanda roxburghii. Advances in Pharmacological and Pharmaceutical Sciences, 2021, 5569054.
    1. Ahmad Nadzri, F. N., Tawalbeh, D., & Sarbon, N. M. (2021). Physicochemical properties and antioxidant activity of enzymatic hydrolysed chickpea (Cicer arietinum L.) protein as influence by alcalase and papain enzyme. Biocatalysis and agricultural. Biotechnology, 36, 102131.
    1. Ahmadifard, N., Murueta, J. H. C., Abedian-Kenari, A., Motamedzadegan, A., & Jamali, H. (2016). Comparison the effect of three commercial enzymes for enzymatic hydrolysis of two substrates (rice bran protein concentrate and soy-been protein) with SDS-PAGE. Journal of Food Science and Technology, 53(2), 1279-1284.

Publication types

MeSH terms

LinkOut - more resources