A complete workflow for discovering small bioactive peptides in foods by LC-MS/MS: A case study on almonds

Huang, Yu-Ping; Dias, Fernanda Furlan Gonçalves; Bell, Juliana Maria Leite Nóbrega de Moura

doi:10.1016/j.foodchem.2021.130834

Cited by 27 publications

(17 citation statements)

References 38 publications

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“…Also, it was challenging to identify peptides with < amino acid residues using peptidomics. [8][9][10]18 To manage these issues, we developed a comprehensive methodology for investigating short and medium-sized peptides.…”

Section: Resultsmentioning

confidence: 99%

“…The number of b-type and y-type ions decreased significantly as sequences shortened. 9 Our method overcame several limitations; it could be used to further elucidate isomeric peptide structures, thereby reducing misinterpretation and solving identity conflicts. However, with the increase in peptide MWs, the amino acid compositions and sequences of peptides (isomers) become more diverse, making it more challenging and laborious to identify medium-sized peptides based on the traditional method.…”

Section: Resultsmentioning

confidence: 99%

“…edu/). 9,25 PeptideRanker (http://distilldeep.ucd.ie/PeptideRanker/) was used to explore the potential bioactivity of medium-sized peptides at a threshold of 0.7. 25 2.12.…”

Section: Methodsmentioning

confidence: 99%

“…Bioactive peptides generally contain 2–12 amino acid residues, with shorter peptides having higher bioavailability. , Liquid chromatography–mass spectrometry/mass spectrometry (LC–MS/MS) is currently the main approach for separating and identifying peptides in complex matrices. Medium-sized peptides have been studied over the past years using peptidomics. − As a subfield of the proteomics, peptidomics methods are increasingly important in food research and have been recently used for bioactive peptide research. , Protein database searches and de novo sequencing strategies are widely used peptidomics methods and rapidly identify huge numbers of peptides.…”

Section: Introductionmentioning

confidence: 99%

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Comprehensive Identification of Short and Medium-Sized Peptides from Pixian Broad Bean Paste Protein Hydrolysates Using UPLC-Q–TOF–MS and UHPLC-Q Exactive HF-X

Fan

2022

J. Agric. Food Chem.

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Pixian broad bean paste (PBBP) is an indispensable food widely used in many East Asian countries, yet the knowledge about bioactive peptides released from parent proteins by enzymatic hydrolysis is limited. A total of 5867 low-molecular weight peptides were identified in the highly bioactive subfractions of the PBBP alcalase hydrolysates using traditional and peptidomics approaches. 19 short peptides (3−5 amino acids) were identified by ultra-performance liquid chromatography quadrupole time-of-flight mass spectrometry, including 5 tripeptides, 8 tetrapeptides, and 6 pentapeptides. 5848 medium-sized peptides (6−10 amino acids) were characterized using the peptidomics approach, including 1484 hexapeptides, 1217 heptapeptides, 1634 octapeptides, 927 nonapeptides, and 586 decapeptides. The comprehensive method can be used for the investigation of bioactive peptides in complex food matrices.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

“…edu/). 9,25 PeptideRanker (http://distilldeep.ucd.ie/PeptideRanker/) was used to explore the potential bioactivity of medium-sized peptides at a threshold of 0.7. 25 2.12.…”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Comprehensive Identification of Short and Medium-Sized Peptides from Pixian Broad Bean Paste Protein Hydrolysates Using UPLC-Q–TOF–MS and UHPLC-Q Exactive HF-X

Fan

2022

J. Agric. Food Chem.

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“…In general, a lower number of peptides were identified in PPHs produced using Neut, although more than 10,000 peptides were identified in all PPHs (Table 4). This is a tremendous increase in depth of analysis compared to previous reports of LC-MS/MS analysis on hydrolysates, where the number of identified peptides is often reported in the tens to low thousands range (Caron et al, 2016;Cui, Sun, Cheng, & Guo, 2022;Hinnenkamp & Ismail, 2021;Y. P. Huang, Dias, Leite Nobrega de Moura Bell, & Barile, 2022;Jin, Yan, Yu, & Qi, 2015;M.…”

Section: 4peptide Identification and Mean Peptide Propertiesmentioning

confidence: 98%

Targeted hydrolysis of native potato protein: A novel route for obtaining hydrolysates with improved interfacial properties

Gregersen

Jafarpour

Yeşiltaş

et al. 2022

Preprint

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Peptides and protein hydrolysates are promising alternatives to substitute chemical additives as functional food ingredients. In this study, we present a novel approach for producing a potato protein hydrolysate with improved emulsifying and foaming properties by data-driven, targeted hydrolysis. Based on previous studies, we selected 15 emulsifier peptides derived from abundant potato proteins, which were clustered based on sequence identity. Through in silico analysis, we determined that from a range of industrial proteases (Neutrase (Neut), Alcalase (Alc), Flavorzyme (Flav) and Trypsin (Tryp)), Tryp was found more likely to release peptides resembling the target peptides. After applying all proteases individually, hydrolysates were assayed for in vitro emulsifying and foaming properties. No direct correlation between degree of hydrolysis and interfacial properties was found. Tryp produced a hydrolysate (DH=5.4%) with the highest (P<0.05) emulsifying and foaming abilities, good stabilities, and high aqueous solubility. Using LC-MS/MS, we identified >10,000 peptides in each hydrolysate. Through peptide mapping, we show that random overlapping with known peptide emulsifiers is not sufficient to quantitatively describe hydrolysate functionality. While Neut hydrolysates had the highest proportion of peptides with target overlap, they showed inferior interfacial activity. In contrast, Tryp was able to release specifically targeted peptides, explaining the high surface activity observed. While modest yields and residual unhydrolyzed protein indicate room for process improvement, this work shows that data-driven, targeted hydrolysis is a viable, interdisciplinary approach to facilitate hydrolysis design for production of functional hydrolysates from alternative protein sources.

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Preparation, characterization, identification, and antioxidant properties of fermented acaí (Euterpe oleracea)

Wen‐Ying

Wang²,

Ren

et al. 2023

Food Science & Nutrition

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Fermentation technology was used to prepare the acaí (Euterpe oleracea) fermentation liquid. The optimal fermentation parameters included a strain ratio of Lactobacillus paracasei: Leuconostoc mesenteroides: Lactobacillus plantarum = 0.5:1:1.5, a fermentation time of 6 days, and a nitrogen source supplemental level of 2.5%. In optimal conditions, the ORAC value of the fermentation liquid reached the highest value of 273.28 ± 6.55 μmol/L Trolox, which was 55.85% higher than the raw liquid. In addition, the FRAP value of the acaí, as well as its scavenging ability of DPPH, hydroxyl, and ABTS free radicals, increased after fermentation. Furthermore, after fermentation treatment, the microstructure, basic physicochemical composition, amino acid composition, γ‐aminobutyric acid, a variety of volatile components, and so on have changed. Therefore, fermentation treatment can significantly improve the nutritional value and flavor of the acaí. This provides a theoretical basis for the comprehensive utilization of acaí.

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A complete workflow for discovering small bioactive peptides in foods by LC-MS/MS: A case study on almonds

Cited by 27 publications

References 38 publications

Comprehensive Identification of Short and Medium-Sized Peptides from Pixian Broad Bean Paste Protein Hydrolysates Using UPLC-Q–TOF–MS and UHPLC-Q Exactive HF-X

Comprehensive Identification of Short and Medium-Sized Peptides from Pixian Broad Bean Paste Protein Hydrolysates Using UPLC-Q–TOF–MS and UHPLC-Q Exactive HF-X

Targeted hydrolysis of native potato protein: A novel route for obtaining hydrolysates with improved interfacial properties

Preparation, characterization, identification, and antioxidant properties of fermented acaí (Euterpe oleracea)

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