PMID- 36306915 OWN - NLM STAT- MEDLINE DCOM- 20221221 LR - 20231213 IS - 1879-0003 (Electronic) IS - 0141-8130 (Linking) VI - 224 DP - 2023 Jan 1 TI - Effect of proanthocyanidins on protein composition, conformational structure, IgE binding capacities and functional properties in soybean protein. PG - 881-892 LID - S0141-8130(22)02416-3 [pii] LID - 10.1016/j.ijbiomac.2022.10.174 [doi] AB - This study was performed to determine the crosslinking formed by proanthocyanidins (PC) with respect to IgE binding capacities, functionality, structure and composition of soybean protein (SPI) following the alkali treatment at 60-100 degrees C. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed the formation of >180 kDa polymers, resulting from the formation of SPI-PC conjugates and protein cross-links. Structural analyses demonstrated that SPI-PC conjugates exhibited structural changes to unfold proteins and increase molecular flexibility. Liquid chromatography coupled to tandem mass spectrometry (LC/MS-MS) showed a decrease in unique protein and peptide numbers as well as major allergen and dominant epitopes abundance. When SPI was treated with PC under the alkali treatment at 80 degrees C, it exhibited a maximum reduction (68.8 %) in the immunoglobulin E (IgE) binding capacity and a maximum increase in DPPH radical scavenging activities (6.11-fold), ABTS + radical scavenging activities (4.80-fold), foaming stability (6.1 %) and emulsifying activity (27.3 %), compared to the control SPI. Overall, this study demonstrates that alkali treatment at 60-100 degrees C to form SPI-PC conjugates has potential applications for producing hypoallergenic soybean products with the desired functionality, most especially from alkali treatment at 80 degrees C. Moreover, the addition of PC pronouncedly alleviates the undesirable functional properties in heated SPI. CI - Copyright (c) 2022 Elsevier B.V. All rights reserved. FAU - Pi, Xiaowen AU - Pi X AD - Northeast Agricultural University, Harbin, Heilongjiang 150030, China. FAU - Liu, Jiafei AU - Liu J AD - Northeast Agricultural University, Harbin, Heilongjiang 150030, China. FAU - Sun, Yuxue AU - Sun Y AD - Northeast Agricultural University, Harbin, Heilongjiang 150030, China; Key Laboratory of Soybean Biology of Chinese Education Ministry, Harbin 150030, China. FAU - Ban, Qingfeng AU - Ban Q AD - Northeast Agricultural University, Harbin, Heilongjiang 150030, China. FAU - Liang, Shuxia AU - Liang S AD - Northeast Agricultural University, Harbin, Heilongjiang 150030, China; Jiangsu DAISY FSMP Co., Ltd, Nantong, Jiangsu 226133, China. FAU - Cheng, Jianjun AU - Cheng J AD - Northeast Agricultural University, Harbin, Heilongjiang 150030, China. Electronic address: jjcheng@neau.edu.cn. FAU - Guo, Mingruo AU - Guo M AD - Department of Nutrition and Food Science, College of Agriculture and Life Sciences, University of Vermont, Burlington 05405, United States. Electronic address: mguo@uvm.edu. LA - eng PT - Journal Article DEP - 20221025 PL - Netherlands TA - Int J Biol Macromol JT - International journal of biological macromolecules JID - 7909578 RN - 0 (Soybean Proteins) RN - 0 (Proanthocyanidins) RN - 37341-29-0 (Immunoglobulin E) SB - IM MH - *Soybean Proteins/chemistry MH - *Proanthocyanidins MH - Immunoglobulin E MH - Glycine max/chemistry MH - Hot Temperature OTO - NOTNLM OT - Composition OT - Functionality OT - IgE binding capacities OT - Proanthocyanidins OT - Soybean protein OT - Structure COIS- Declaration of competing interest All authors declare no conflict of interest. EDAT- 2022/10/29 06:00 MHDA- 2022/12/22 06:00 CRDT- 2022/10/28 19:24 PHST- 2022/08/30 00:00 [received] PHST- 2022/10/12 00:00 [revised] PHST- 2022/10/20 00:00 [accepted] PHST- 2022/10/29 06:00 [pubmed] PHST- 2022/12/22 06:00 [medline] PHST- 2022/10/28 19:24 [entrez] AID - S0141-8130(22)02416-3 [pii] AID - 10.1016/j.ijbiomac.2022.10.174 [doi] PST - ppublish SO - Int J Biol Macromol. 2023 Jan 1;224:881-892. doi: 10.1016/j.ijbiomac.2022.10.174. Epub 2022 Oct 25.