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脉冲蛋白水解物经固定化金属亲和分离后的冰晶重结晶抑制活性。

Ice recrystallization inhibition activity of pulse protein hydrolysates after immobilized metal affinity separation.

机构信息

Department of Food Science, The University of Tennessee, 2510 River Dr, Knoxville, TN 37996-4539, USA.

Institute for Advanced Materials and Manufacturing, The University of Tennessee, 2641 Osprey Vista Way, Knoxville, TN 37920, USA.

出版信息

Food Chem. 2024 Dec 1;460(Pt 2):140574. doi: 10.1016/j.foodchem.2024.140574. Epub 2024 Jul 29.

DOI:10.1016/j.foodchem.2024.140574
PMID:39089028
Abstract

Creating molecules capable of inhibiting ice recrystallization is an active research area aiming to improve the freeze-thaw characteristics of foods and biomedical materials. Peptide mixtures have shown promise in preventing freezing-induced damage, but less is known about the relationship between their amino acid compositions and ice recrystallization inhibition (IRI) activities. In this article, we used Ni immobilized metal affinity chromatography (IMAC) to fractionate pulse protein hydrolysates, created by Alcalase and trypsin, into mixtures lacking and enriched in His, and Cys residues. The aim of this study was to fractionate pulse protein hydrolysates based on their amino acid compositions and evaluate their resulting physicochemical and IRI characteristics. Ni IMAC fractionation induced IRI activity in all of the evaluated soy, chickpea, and pea protein hydrolysates regardless of their amino acid composition. Ni IMAC fractionation produced chemically distinct fractions of peptides, differing by their molecular weights, amino acid composition, and IRI activities. The resulting peptide mixtures' molecular weight, amino acid composition, secondary structure, and sodium ion levels were found to have no correlation with their IRI activities. Thus, we demonstrate for the first time the ability of Ni IMAC fractionation to induce IRI activity in hydrolyzed pulse proteins.

摘要

开发抑制冰晶重结晶的分子是一个活跃的研究领域,旨在改善食品和生物医学材料的抗冻融特性。肽混合物在预防冷冻诱导损伤方面显示出了潜力,但关于它们的氨基酸组成与冰晶重结晶抑制(IRI)活性之间的关系,人们知之甚少。在本文中,我们使用 Ni 固定化金属亲和层析(IMAC)将由 Alcalase 和胰蛋白酶产生的脉冲蛋白水解物分成缺乏和富含 His 和 Cys 残基的混合物。本研究的目的是根据氨基酸组成对脉冲蛋白水解物进行分级,并评估其理化性质和 IRI 特性。无论氨基酸组成如何,Ni IMAC 分级都会诱导所有评估的大豆、鹰嘴豆和豌豆蛋白水解物的 IRI 活性。Ni IMAC 分级产生了化学性质不同的肽级分,它们的分子量、氨基酸组成和 IRI 活性不同。结果表明,所得肽混合物的分子量、氨基酸组成、二级结构和钠离子水平与 IRI 活性之间没有相关性。因此,我们首次证明了 Ni IMAC 分级能够在水解的脉冲蛋白中诱导 IRI 活性。

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