Peptidomics: new trends in food science

Martini, Serena; Solieri, Lisa; Tagliazucchi, Davide

doi:10.1016/j.cofs.2020.12.016

Cited by 47 publications

(22 citation statements)

References 63 publications

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“…The F4 fraction was selected for peptidomic investigation for its high biological potential (ACE-inhibitory and antioxidant activities) and for the presence of short peptide sequences, which are actually less susceptible to the action of gastrointestinal and brush-border proteases and, thus, potentially bioavailable. 36 The full list of identified peptides as well as the mass spectrometry data is provided in Table S1 . A total of 239 peptides having 2 to 9 amino acid residues and 4 free amino acids were detected in fraction F4.…”

Section: Results and Discussionmentioning

confidence: 99%

“…With the aim to identify alleged bioactive peptides, fraction F4 was subjected to high-resolution mass spectrometry analysis. The F4 fraction was selected for peptidomic investigation for its high biological potential (ACE-inhibitory and antioxidant activities) and for the presence of short peptide sequences, which are actually less susceptible to the action of gastrointestinal and brush-border proteases and, thus, potentially bioavailable . The full list of identified peptides as well as the mass spectrometry data is provided in Table S1.…”

Section: Results and Discussionmentioning

confidence: 99%

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Antioxidant and Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides Obtained from Alcalase Protein Hydrolysate Fractions of Hemp (Cannabis sativa L.) Bran

Samaei

Martini

Tagliazucchi

et al. 2021

J. Agric. Food Chem.

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Proteins from hemp bran (HPB), a byproduct of the hemp seed food-processing chain, were chemically extracted, hydrolyzed by Alcalase, and separated by membrane ultrafiltration into four fractions (MW <1, 1–3, 3–5, and >5 kDa). The antioxidant and antihypertensive properties of the initial extract and the fractions were evaluated by in vitro assays for their ability to scavenge radical species, bind with metal ions, reduce ferric ions, and inhibit angiotensin-converting enzyme (ACE) activity. Bioactive peptides were identified by high-resolution mass spectrometry and sequence comparison with BIOPEP and BioPep DB databases. The hydrolysate was strongly antioxidant and ACE-inhibiting; the most bioactive peptides were further concentrated by ultrafiltration. Of the 239 peptides identified, 47 (12 antioxidant and 35 ACE-inhibitory) exhibited structural features correlated with the specific bioactivity. These results highlight the promise of hydrolysate and size-based HPB fractions as natural functional ingredients for the food or pharmaceutical industry.

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Section: Results and Discussionmentioning

confidence: 99%

Section: Results and Discussionmentioning

confidence: 99%

Antioxidant and Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides Obtained from Alcalase Protein Hydrolysate Fractions of Hemp (Cannabis sativa L.) Bran

Samaei

Martini

Tagliazucchi

et al. 2021

J. Agric. Food Chem.

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“…The proteome is a dynamic reflection of genes/transcripts and the environment, and it has been used for biomarker discovery in clinical diagnosis, to study the effects of nutrients on human protein expression, the changes in food under certain conditions, or for the identification and validation of bioactive food peptides and their health effects. 46 A variety of proteomic approaches for reliable quantification of individual proteins and/or food proteome are available, and they have been widely applied in food research, quality control, authenticity assessment, safety control, and food bioactivity. 47 The expansion of proteomics in the food science field has been possible, because of the application of high-resolving separation systems (mainly liquid chromatography (LC)), together with high sensitivity and high-resolution (HR) tandem mass spectrometry (MS).…”

Section: T H Imentioning

confidence: 99%

Foodomics: Analytical Opportunities and Challenges

et al. 2021

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“…This can be achieved by using purified enzymes, microorganisms or through in vitro digestion [1,2,5]. Next, untargeted peptidomics is applied to identify all the peptides present in the sample [20]. The list obtained represents the pool of peptides that can be used for the subsequent in silico screening.…”

Section: Introductionmentioning

confidence: 99%

Application of a Combined Peptidomics and In Silico Approach for the Identification of Novel Dipeptidyl Peptidase-IV-Inhibitory Peptides in In Vitro Digested Pinto Bean Protein Extract

Martini

Cattivelli

Conte

et al. 2021

CIMB

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The conventional approach in bioactive peptides discovery, which includes extensive bioassay-guided fractionation and purification processes, is tedious, time-consuming and not always successful. The recently developed bioinformatics-driven in silico approach is rapid and cost-effective; however, it lacks an actual physiological significance. In this study a new integrated peptidomics and in silico method, which combines the advantages of the conventional and in silico approaches by using the pool of peptides identified in a food hydrolysate as the starting point for subsequent application of selected bioinformatics tools, has been developed. Pinto bean protein extract was in vitro digested and peptides were identified by peptidomics. The pool of obtained peptides was screened by in silico analysis and structure–activity relationship modelling. Three peptides (SIPR, SAPI and FVPH) were selected as potential inhibitors of the dipeptidyl-peptidase-IV (DPP-IV) enzyme by this integrated approach. In vitro bioactivity assay showed that all three peptides were able to inhibit DPP-IV with the tetra-peptide SAPI showing the highest activity (IC50 = 57.7 μmol/L). Indeed, a new possible characteristic of peptides (i.e., the presence of an S residue at the N-terminus) able to inhibit DPP-IV was proposed.

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Peptidomics: new trends in food science

Cited by 47 publications

References 63 publications

Antioxidant and Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides Obtained from Alcalase Protein Hydrolysate Fractions of Hemp (Cannabis sativa L.) Bran

Antioxidant and Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides Obtained from Alcalase Protein Hydrolysate Fractions of Hemp (Cannabis sativa L.) Bran

Foodomics: Analytical Opportunities and Challenges

Application of a Combined Peptidomics and In Silico Approach for the Identification of Novel Dipeptidyl Peptidase-IV-Inhibitory Peptides in In Vitro Digested Pinto Bean Protein Extract

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