Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Biofunctionality of Enzymatically Derived Peptides from Codfish (Gadus morhua) Frame: Bulk in vitro Properties, Quantitative Proteomics, and Bioinformatic Prediction

Ali Jafarpour
* ORCID logo ,
Simon Gregersen
* ORCID logo ,
Rocio Marciel Gomes
,
Paolo Marcatili
,
Tobias Hegelund Olsen
ORCID logo ,
Charlotte Jacobsen
ORCID logo ,
Michael T. Overgaard
,
Ann Dorit Moltke Sørensen
Version 1 : Received: 3 November 2020 / Approved: 4 November 2020 / Online: 4 November 2020 (12:44:08 CET)

A peer-reviewed article of this Preprint also exists.

Jafarpour, A.; Gregersen, S.; Marciel Gomes, R.; Marcatili, P.; Hegelund Olsen, T.; Jacobsen, C.; Overgaard, M.T.; Sørensen, A.-D.M. Biofunctionality of Enzymatically Derived Peptides from Codfish (Gadus morhua) Frame: Bulk In Vitro Properties, Quantitative Proteomics, and Bioinformatic Prediction. Mar. Drugs 2020, 18, 599. Jafarpour, A.; Gregersen, S.; Marciel Gomes, R.; Marcatili, P.; Hegelund Olsen, T.; Jacobsen, C.; Overgaard, M.T.; Sørensen, A.-D.M. Biofunctionality of Enzymatically Derived Peptides from Codfish (Gadus morhua) Frame: Bulk In Vitro Properties, Quantitative Proteomics, and Bioinformatic Prediction. Mar. Drugs 2020, 18, 599.

Abstract

Protein hydrolysates show great promise as bioactive food and feed ingredient and for valorization of side-streams from e.g. the fish processing industry. This study characterizes bulk emulsifying, foaming, and in vitro antioxidative properties of hydrolysates derived from cod frame by application of Alcalase and Neutrase, individually and sequentially as well as the influence of heat-treatment prior to hydrolysis. We present a novel approach that utilizes proteomics data for calculation of weighted mean peptide properties (length, molecular weight, and charge) and peptide-level abundance estimation. Using subsequent bioinformatic prediction of biofunctional properties to describe observed bulk properties, we are able to provide an in-depth hydrolysate characterization not previously seen. All hydrolysates displayed comparable or higher emulsifying activity and stability than sodium caseinate. Heat-treatment significantly increased stability but showed a negative effect on the activity and degree of hydrolysis. Combining peptide abundance with predicted emulsifying activity, we were able to identify several peptides that are likely linked to the observed differences in bulk emulsifying properties. In general, decreased hydrolysis resulted in significantly higher chelating activity, while the opposite was observed for radical scavenging activity. The study highlights the prospects of applying proteomics and bioinformatics for hydrolysate characterization and in food protein science.

Keywords

codfish; enzymatic hydrolysis; proteomics; bioinformatic prediction; emulsifying properties; antioxidative activity; bioactive peptides

Subject

Chemistry and Materials Science, Analytical Chemistry

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Download PDF Download Supplementary

Comments (0)

We encourage comments and feedback from a broad range of readers. See criteria for comments and our Diversity statement.

Leave a public comment
Send a private comment to the author(s)
* All users must log in before leaving a comment
Views 0
Downloads 0
Comments 0
Metrics 0
Get PDF Supplementary Files Cite Share 0
Bookmark BibSonomy Mendeley Reddit Delicious
×
Alerts
Notify me about updates to this article or when a peer-reviewed version is published.
We use cookies on our website to ensure you get the best experience.
Read more about our cookies here.