Characterization of endogenous endopeptidases and exopeptidases and application for the limited hydrolysis of peanut proteins.
Ara h 1
Arachin
Cleavage site
Endogenous proteases
IgE-binding epitope
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
30 May 2021
30 May 2021
Historique:
received:
16
07
2020
revised:
03
11
2020
accepted:
28
11
2020
pubmed:
15
12
2020
medline:
1
4
2021
entrez:
14
12
2020
Statut:
ppublish
Résumé
Research concerning the utilization of oilseed endogenous proteases is scarce. Herein, we investigated the peanut proteases and their effects on peanut proteins. Liquid chromatography tandem mass spectrometry analysis showed that peanut contained several endopeptidases and exopeptidases. Protease inhibitor assay and analysis of cleavage sites showed that the obvious proteolytic activity at pH 2-5 and 20-60 °C was from aspartic endopeptidases (optimal at pH 3) and one legumain (pH 4). The above endopeptidases destroyed five and six IgE-binding epitopes of Ara h 1 at pH 3 and 4, respectively. Ara h 1 (>95%) and arachin (50-60%) could be hydrolyzed to generate 10-20 kDa and <4 kDa peptides at pH 3, which was enhanced by the pH 3 → 4 incubation. Further, the limited hydrolysis improved the gel-forming ability and in vitro digestibility (approximately 15%) of peanut proteins. Free amino acid analysis showed that the activity of exopeptidases was low at pH 2-5.
Identifiants
pubmed: 33310254
pii: S0308-8146(20)32626-1
doi: 10.1016/j.foodchem.2020.128764
pii:
doi:
Substances chimiques
Allergens
0
Antigens, Plant
0
Epitopes
0
Peptides
0
Endopeptidases
EC 3.4.-
Exopeptidases
EC 3.4.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
128764Informations de copyright
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