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Proteomics and bioinformatics guided discovery of microalgal multifunctional peptides for novel nutraceutical applications

ABSTRACT: This study aimed to identify and characterize bioactive peptides derived from protein hydrolysates of Arthrospira platensis (APPH) and Tetraselmis chuii (TCPH) using an integrated peptidomics and bioinformatics approach. Proteins extracted from the microalgae were hydrolyzed using pepsin (EC 3.4.23.1) at various enzyme/substrate (E/S) ratios. APPH and TCPH, prepared at an E/S ratio of 1/10 (w/w), were analyzed using peptidomics through reverse-phase high-performance liquid chromatography (RP-HPLC) coupled with tandem mass spectrometry (MS/MS). Using the UniProtKB database, a total of 265 unique peptides were identified, including 187 peptides from APPH and 78 peptides from TCPH. Subsequent in silico analysis of these peptides revealed favorable physicochemical properties, with a notable distribution of hydrophobic (APPH: 26; TCPH: 5), amphipathic (APPH: 70; TCPH: 16), and hydrophilic peptides (APPH: 59; TCPH: 17). Toxicity assessments confirmed that none of the peptides showed hemolytic or cytotoxic risks, except for one peptide identified in TCPH with potential cytotoxicity. Furthermore, bioactivity predictions demonstrated significant multifunctional properties (scores exceeding the 0.500 threshold), identifying peptides with antihypertensive (APPH: 2; TCPH: 1), anti-diabetic (APPH: 2), anti-inflammatory (APPH: 14; TCPH: 5) and antimicrobial (APPH: 7) activities. The current study thus establishes protein hydrolysates from A. platensis and T. chuii as promising sources of bioactive peptides suitable for nutraceutical applications. Our integrated analytical and computational strategy provides critical insights into peptide multifunctionality, supporting further research and development of microalgae-derived peptides.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Arthrospira Platensis Tetraselmis Chuii

TISSUE(S): Photosynthetic Cell

SUBMITTER: Barbara Deracinois

LAB HEAD: Jean-Louis Hilbert

PROVIDER: PXD058907 | Pride | 2025-07-09

REPOSITORIES: Pride

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Project 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.

Project description:Genetic dissection of the S rat genome has provided strong evidence for the presence of two interacting blood pressure (BP) quantitative trait loci (QTLs), termed QTL1 and QTL2, on rat chromosome 5. However, the identities of the underlying interacting genetic factors remain unknown. Further experiments targeted to identify the interacting genetic factors by the substitution mapping approach alone are difficult because of the interdependency of natural recombinations to occur at the two QTLs. We hypothesized that the interacting genetic factors underlying these two QTLs may interact at the level of gene transcription and thereby represent expression QTLs (eQTLs). To detect these interacting eQTLs, a custom QTL chip containing the annotated genes within QTL1 and QTL2 was developed and used to conduct a transcriptional profiling study of S and two congenic strains that retain either one or both the QTLs. The results uncovered an interaction between two transcription factors, DMRTA2 and NFIA. Further, the âbiological signatureâ elicited by these two transcription factors was differential between the congenic strain that retained LEW alleles at both QTL1 and 2 compared to the congenic strain that retained LEW alleles at QTL1 alone. A network of transcription factors potentially affecting BP could be traced, lending support to our hypothesis. Pairs of Cy5 and Cy3 labeled targets were co-hybridized onto either a custom long oligonucleotide microarray for the interrogation of 231 genes encompassed by QTL1 and QTL2, or a TIGR rat cDNA array consisting of 26,401 probe elements representing 20,465 unique non-QTL genes. A âflip-dyeâ or âbalanced blockâ design was used as the experimental method of choice to account for potential dye-bias labeling effects. Six âbalanced blockâ normalized files are submitted for the long oligonucleotide array interrogating the hearts from S versus S.LEW(5)x6x9 animals, fourteen âflip-dyeâ hybridizations are submitted for the cDNA array interrogating the hearts from S versus S.LEW(5)x6x9 animals, and twelve âflip-dyeâ hybridizations are submitted for the cDNA array interrogating the hearts from S versus S.LEW(5)x6x11 animals. GPR and MEV files cannot be located.

			Action	DRS
	APPH.7z	Other
	APPH_Aplatensis_protein-peptides.csv	Csv
	APPH_SwissProt_protein-peptides.csv	Csv
	APPH_Tchuii_protein-peptides.csv	Csv
	TCPH.7z	Other

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Proteomics and bioinformatics guided discovery of microalgal multifunctional peptides for novel nutraceutical applications

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