Enzymatic modification of oat globulin enables covalent interaction with procyanidin B2

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Korpela , B , Pitkänen , L & Heinonen , M 2022 , ' Enzymatic modification of oat globulin enables covalent interaction with procyanidin B2 ' , Food Chemistry , vol. 395 , 133568 . https://doi.org/10.1016/j.foodchem.2022.133568

Title: Enzymatic modification of oat globulin enables covalent interaction with procyanidin B2
Author: Korpela, Bei; Pitkänen, Leena; Heinonen, Marina
Contributor organization: Food Quality & Safety
Department of Food and Nutrition
University of Helsinki
Carbohydrate Chemistry and Enzymology
Helsinki One Health (HOH)
Date: 2022-11-30
Language: eng
Number of pages: 10
Belongs to series: Food Chemistry
ISSN: 0308-8146
DOI: https://doi.org/10.1016/j.foodchem.2022.133568
URI: http://hdl.handle.net/10138/346721
Abstract: The effect of enzyme treatment on protein-tannin interactions was investigated using up-to-date analytical approaches for improving their physical properties. The formation of ligands between procyanidin B2 and native oat globulin (OG) was observed to be affected by the ratio of procyanidin B2 to OG and the availability of tryptophan. For the transglutaminase-treated OG, the results obtained from circular dichroism (CD) and size exclusion chromatography (SEC) revealed that procyanidin B2 acted as an acyl acceptor in the process of OG deamidation. Procyanidin B2 also inhibited the non-covalent protein-protein interactions occurring between the aromatic side-chains or sedimentation of tryptophan aggregates. For trypsin-treated OG, procyanidin B2 interacted with phenylalanine and the tryptophan side-chain of OG. The inhibition of procyanidin B2 towards protein-protein aggregation was proved by the observation of CD, SEC and asymmetric flow field-flow fractionation.
Subject: Protein-tannin interaction
Oat protein
Phenolics
Circular dichroism
Size exclusion
AF4-MALS-RI
FUNCTIONAL-PROPERTIES
CIRCULAR-DICHROISM
PHENOLIC-COMPOUNDS
PROTEIN
SEED
TRANSGLUTAMINASE
BOVINE
MILK
FABA
416 Food Science
Peer reviewed: Yes
Rights: cc_by
Usage restriction: openAccess
Self-archived version: publishedVersion


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