Enzymatic modification of oat globulin enables covalent interaction with procyanidin B2.

Bei Korpela, Leena Pitkänen, Marina Heinonen

Food chemistry 2022 Nov 30

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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. Copyright © 2022 The Authors. Published by Elsevier Ltd.. All rights reserved.

Citation

Bei Korpela, Leena Pitkänen, Marina Heinonen. Enzymatic modification of oat globulin enables covalent interaction with procyanidin B2. Food chemistry. 2022 Nov 30;395:133568