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豌豆谷蛋白与亲脂性生物活性化合物的分子相互作用:结构-结合关系及纳米/微络合

Molecular Interaction of Pea Glutelin and Lipophilic Bioactive Compounds: Structure-Binding Relationship and Nano-/Microcomplexation.

作者信息

Okagu Ogadimma D, Abioye Raliat O, Udenigwe Chibuike C

机构信息

Department of Chemistry and Biomolecular Sciences, Faculty of Science, University of Ottawa, Ottawa, Ontario K1N 6N5, Canada.

School of Nutrition Sciences, Faculty of Health Sciences, University of Ottawa, Ottawa, Ontario K1H 8M5, Canada.

出版信息

J Agric Food Chem. 2023 Mar 29;71(12):4957-4969. doi: 10.1021/acs.jafc.3c00047. Epub 2023 Mar 20.

DOI:10.1021/acs.jafc.3c00047
PMID:36939737
Abstract

This study investigated the impact of ionic strength and lipophilicity of bioactive compounds on their interaction with the alkaline soluble pea glutelin fraction (ASF) using the fluorescence quenching technique. A Stern-Volmer quenching constant, , of 8.9 ± 0.10, 5.3 ± 0.06, 4.0 ± 0.01, 1.1 ± 0.00, 0.9 ± 0.02, and 0.1 ± 0.00 (×10 M) was observed for curcumin-ASF (CuASF), astaxanthin-ASF (AsASF), cholecalciferol-ASF (ChASF), β-carotene-ASF (βCaASF), coenzyme Q-ASF (QASF), and β-sitosterol-ASF (βSiASF) complexes, respectively. An increase in ionic strength did not significantly change , the effective quenching constant , and the bimolecular quenching rate constant . However, it changed the mode of interaction of the ASF with cholecalciferol, β-carotene, coenzyme Q, and β-sitosterol from static to static-dynamic quenching. Transmission electron microscopy showed that the morphology formed with protein (spherical nanocomplexes, microaggregates, or fiber-like particles) differed among the compounds. The favorable binding of CuASF, AsASF, ChASF, and βCaASF complexes provides stable matrices for formulating protein-based delivery systems for lipophilic nutraceuticals.

摘要

本研究采用荧光猝灭技术,研究了生物活性化合物的离子强度和亲脂性对其与碱性可溶豌豆谷蛋白组分(ASF)相互作用的影响。姜黄素-ASF(CuASF)、虾青素-ASF(AsASF)、胆钙化醇-ASF(ChASF)、β-胡萝卜素-ASF(βCaASF)、辅酶Q-ASF(QASF)和β-谷甾醇-ASF(βSiASF)复合物的斯特恩-沃尔默猝灭常数(K_{sv})分别为8.9±0.10、5.3±0.06、4.0±0.01、1.1±0.00、0.9±0.02和0.1±0.00(×10(^6) M)。离子强度的增加并没有显著改变有效猝灭常数(K_{eff})和双分子猝灭速率常数(k_q)。然而,它改变了ASF与胆钙化醇、β-胡萝卜素、辅酶Q和β-谷甾醇的相互作用模式,从静态猝灭变为静态-动态猝灭。透射电子显微镜显示,不同化合物形成的蛋白质形态(球形纳米复合物、微聚集体或纤维状颗粒)有所不同。CuASF、AsASF、ChASF和βCaASF复合物的良好结合为亲脂性营养保健品的蛋白质递送系统提供了稳定的基质。

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