2020
Santos-Hernández, Marta; Alfieri, Fabio; Gallo, Veronica; Miralles, Beatriz; Masi, Paolo; Romano, Annalisa; Ferranti, Pasquale; Recio, Isidra
Compared digestibility of plant protein isolates by using the INFOGEST digestion protocol Artículo de revista
En: Food Research International, vol. 137, pp. 109708, 2020, ISSN: 0963-9969.
Resumen | Enlaces | BibTeX | Etiquetas: Casein, Epitopes, Garden pea, Gastrointestinal digestion, Grass pea, Lentil, Protein isolate, Soybean, Whey protein
@article{SANTOSHERNANDEZ2020109708,
title = {Compared digestibility of plant protein isolates by using the INFOGEST digestion protocol},
author = {Marta Santos-Hernández and Fabio Alfieri and Veronica Gallo and Beatriz Miralles and Paolo Masi and Annalisa Romano and Pasquale Ferranti and Isidra Recio},
url = {https://www.sciencedirect.com/science/article/pii/S096399692030733X},
doi = {https://doi.org/10.1016/j.foodres.2020.109708},
issn = {0963-9969},
year = {2020},
date = {2020-01-01},
urldate = {2020-01-01},
journal = {Food Research International},
volume = {137},
pages = {109708},
abstract = {The use of ingredients based on plant protein isolates is being promoted due to sustainability and health reasons. However, it is necessary to explore the behaviour of plant protein isolates during gastrointestinal digestion including the profile of released free amino acids and the characterization of resistant domains to gastrointestinal digestion. The aim of the present study was to monitor protein degradation of four legume protein isolates: garden pea, grass pea, soybean and lentil, using the harmonized Infogest in vitro digestion protocol. In vitro digests were characterized regarding protein, peptide and free amino acid content. Soybean was the protein isolate with the highest percentage of insoluble nitrogen at the end of the digestion (12%), being this fraction rich in hydrophobic amino acids. Free amino acids were mainly released during the intestinal digestion, comprising 21–24% of the total nitrogen content, while the percentage of nitrogen corresponding to peptides ranged from 66 to 76%. Legume globulins were resistant to gastric digestion whereas they were hydrolysed into peptides and amino acids during the intestinal phase. However, the molecular weight (MW) distribution demonstrated that all intestinal digests, except those from soybean, contained peptides with MW > 4 kDa at the end of gastrointestinal digestion. The profile of free amino acids released during digestion supports legume protein isolates as an excellent source of essential amino acids to be used in protein-rich food products. Peptides released during digestion matched with previously reported epitopes from the same plant species or others, explaining the ability to induce allergic reactions and cross-linked reactivity.},
keywords = {Casein, Epitopes, Garden pea, Gastrointestinal digestion, Grass pea, Lentil, Protein isolate, Soybean, Whey protein},
pubstate = {published},
tppubtype = {article}
}
The use of ingredients based on plant protein isolates is being promoted due to sustainability and health reasons. However, it is necessary to explore the behaviour of plant protein isolates during gastrointestinal digestion including the profile of released free amino acids and the characterization of resistant domains to gastrointestinal digestion. The aim of the present study was to monitor protein degradation of four legume protein isolates: garden pea, grass pea, soybean and lentil, using the harmonized Infogest in vitro digestion protocol. In vitro digests were characterized regarding protein, peptide and free amino acid content. Soybean was the protein isolate with the highest percentage of insoluble nitrogen at the end of the digestion (12%), being this fraction rich in hydrophobic amino acids. Free amino acids were mainly released during the intestinal digestion, comprising 21–24% of the total nitrogen content, while the percentage of nitrogen corresponding to peptides ranged from 66 to 76%. Legume globulins were resistant to gastric digestion whereas they were hydrolysed into peptides and amino acids during the intestinal phase. However, the molecular weight (MW) distribution demonstrated that all intestinal digests, except those from soybean, contained peptides with MW > 4 kDa at the end of gastrointestinal digestion. The profile of free amino acids released during digestion supports legume protein isolates as an excellent source of essential amino acids to be used in protein-rich food products. Peptides released during digestion matched with previously reported epitopes from the same plant species or others, explaining the ability to induce allergic reactions and cross-linked reactivity.
2016
Cruz-Huerta, Elvia; Maqueda, Daniel Martínez; de la Hoz, Lucia; da Silva, Vera S Nunes; Pacheco, Maria Teresa Bertoldo; Amigo, Lourdes; Recio, Isidra
En: J Dairy Sci, vol. 99, no 1, pp. 77–82, 2016, ISSN: 1525-3198.
Resumen | Enlaces | BibTeX | Etiquetas: enzymatic hydrolysis, iron-binding peptide, reversed phase HPLC-tandem mass spectrometry, Whey protein
@article{pmid26601589,
title = {Short communication: Identification of iron-binding peptides from whey protein hydrolysates using iron (III)-immobilized metal ion affinity chromatography and reversed phase-HPLC-tandem mass spectrometry},
author = {Elvia Cruz-Huerta and Daniel Martínez Maqueda and Lucia de la Hoz and Vera S Nunes da Silva and Maria Teresa Bertoldo Pacheco and Lourdes Amigo and Isidra Recio},
doi = {10.3168/jds.2015-9839},
issn = {1525-3198},
year = {2016},
date = {2016-01-01},
urldate = {2016-01-01},
journal = {J Dairy Sci},
volume = {99},
number = {1},
pages = {77--82},
abstract = {Peptides with iron-binding capacity obtained by hydrolysis of whey protein with Alcalase (Novozymes, Araucaria, PR, Brazil), pancreatin, and Flavourzyme (Novozymes) were identified. Hydrolysates were subjected to iron (III)-immobilized metal ion affinity chromatography, and the bound peptides were sequenced by mass spectrometry. Regardless of the enzyme used, the domains f(42-59) and f(125-137) from β-lactoglobulin enclosed most of identified peptides. This trend was less pronounced in the case of peptides derived from α-lactalbumin, with sequences deriving from diverse regions. Iron-bound peptides exhibited common structural characteristics, such as an abundance of Asp, Glu, and Pro, as revealed by mass spectrometry and AA analysis. In conclusion, this characterization of iron-binding peptides helps clarify the relationship between peptide structure and iron-chelating activity and supports the promising role of whey protein hydrolysates as functional ingredients in iron supplementation treatments. },
keywords = {enzymatic hydrolysis, iron-binding peptide, reversed phase HPLC-tandem mass spectrometry, Whey protein},
pubstate = {published},
tppubtype = {article}
}
Peptides with iron-binding capacity obtained by hydrolysis of whey protein with Alcalase (Novozymes, Araucaria, PR, Brazil), pancreatin, and Flavourzyme (Novozymes) were identified. Hydrolysates were subjected to iron (III)-immobilized metal ion affinity chromatography, and the bound peptides were sequenced by mass spectrometry. Regardless of the enzyme used, the domains f(42-59) and f(125-137) from β-lactoglobulin enclosed most of identified peptides. This trend was less pronounced in the case of peptides derived from α-lactalbumin, with sequences deriving from diverse regions. Iron-bound peptides exhibited common structural characteristics, such as an abundance of Asp, Glu, and Pro, as revealed by mass spectrometry and AA analysis. In conclusion, this characterization of iron-binding peptides helps clarify the relationship between peptide structure and iron-chelating activity and supports the promising role of whey protein hydrolysates as functional ingredients in iron supplementation treatments.
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