PXD050312-1

PXD050312 is an original dataset announced via ProteomeXchange.

Title	Metal chelating properties of fractionated potato protein hydrolysates
Description	Metal-catalyzed lipid oxidation is a major factor in food waste, as it reduces shelf life. Addressing this issue, our study investigates the potential of hydrolysates derived from potato protein, a by-product of potato starch production, as metal chelating antioxidants. Through sequential en-zymatic hydrolysis using Alcalase or Trypsin combined with Flavourzyme, we produced various hydrolysates, which were then fractionated via ultrafiltration. Using a combination of peptidomics and bioinformatics, we predicted the presence of metal-chelating and free radical scavenging pep-tides across all hydrolysate fractions, with a trend indicating a higher content of antioxidant pep-tides in lower molecular weight fractions. To validate these predictions, we utilized Surface Plas-mon Resonance (SPR) and a 9-day emulsion storage experiment. While SPR demonstrated poten-tial in identifying antioxidant activity, it faced challenges in differentiating between hydrolysate fractions due to significant standard errors. In the storage experiment, all hydrolysates showed li-pid oxidation inhibition, though not as effectively as EDTA. Remarkably, one fraction (AF13) was not significantly different (p < 0.05) from EDTA in suppressing hexanal formation. These results highlight SPR and peptidomics/bioinformatics as promising yet limited methods for antioxidant screening. Importantly, this study reveals the potential of potato protein hydrolysates as antioxi-dants in food products, warranting further research. The aim of this study was to evaluate the potential of SPR as a screening technique for potato protein hydrolysates (PPH) as metal chelating antioxidants. More specifically, the goal was to correlate the KD of the hydrolysates, determined by SPR, with development of different oxidation markers obtained during a storage experiment where the PPHs were added as antioxidants to 5 % fish oil-in-water emulsions at pH 7. Additionally, the effect of using different combinations of enzymes on antioxidant activity of the hydrolysates was investigated and peptidomics was applied to characterize the composition of the hydroly-sates. With the aim of achieving shorter peptides through a high degree of hydrolysis (DH%), this study utilized sequential hydrolysis, where Trypsin (Try) or Alcalase (Alc) was paired with Flavourzyme (Fla). Owing to its broad specificity as a heterogeneous combination of various endo- and exopeptidases [20], Flavourzyme is known to facilitate high DH% and the production of short peptides [21]. However, it has been reported that when used solely with a denatured substrate protein of limited solubility, Flavourzyme can yield a significantly lower DH% than anticipated [19]. Consequently, this study was designed to include substrate pre-digestion prior to Flavourzyme addition.
HostingRepository	PRIDE
AnnounceDate	2024-06-23
AnnouncementXML	Submission_2024-06-23_02:26:57.288.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD050312
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Simon Gregersen Echers
SpeciesList	scientific name: Solanum tuberosum (Potato); NCBI TaxID: 4113;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2024-03-04 01:36:38	ID requested
⏵ 1	2024-06-23 02:26:58	announced
2	2024-10-22 06:47:17	announced	2024-10-22: Updated project metadata.

10.6019/PXD050312;

10.3390/antiox13030346;

Bj, ø, rlie M, Hartmann JC, Rasmussen LH, Yesiltas B, S, ø, rensen AM, Gregersen Echers S, Jacobsen C, Screening for Metal-Chelating Activity in Potato Protein Hydrolysates Using Surface Plasmon Resonance and Peptidomics. Antioxidants (Basel), 13(3):(2024) [pubmed]

submitter keyword: Potato, AnOxPePred, SPR, sequential hydrolysis, antioxidant activity, hydrolysate

Simon Gregersen Echers
contact affiliation	Department of Chemistry and Bioscience Aalborg University Denmark
contact email	sgr@bio.aau.dk
lab head
Simon Gregersen Echers
contact affiliation	Department of Chemistry & Bioscience Aalborg University
contact email	sgr@bio.aau.dk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD050312
     1. Label: PRIDE project
     2. Name: Metal chelating properties of fractionated potato protein hydrolysates