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苏氨酸酰化玉米醇溶蛋白和明胶水解物可以提高其抑制冰晶重结晶的活性。

Succinylation of zein and gelatin hydrolysates improved their ice recrystallization inhibition activity.

机构信息

Department of Food Science, University of Tennessee Institute of Agriculture, 2510 River Dr., Knoxville, TN 37996, USA.

Department of Food Science, University of Tennessee Institute of Agriculture, 2510 River Dr., Knoxville, TN 37996, USA.

出版信息

Food Chem. 2023 Oct 30;424:136431. doi: 10.1016/j.foodchem.2023.136431. Epub 2023 May 22.

DOI:10.1016/j.foodchem.2023.136431
PMID:37244191
Abstract

The goal of this research was to enhance the ice recrystallization inhibition (IRI) activity of zein and gelatin hydrolysates (ZH and GH, respectively) by succinylation modification. ZH was prepared by Alcalase treatment for 3 h and then modified by succinic anhydride (SA); whereas GH was made by Alcalase hydrolysis for 0.25 h and succinylated by n-octylsuccinic anhydride (OSA). After 0.5 h of annealing at -8 °C at 40 mg/mL, modified hydrolysates decreased the average Feret's diameter of ice crystal from 50.2 μm (polyethylene glycol, negative control) to 28.8 μm (SA modified ZH) and 29.5 μm (OSA modified GH) in comparison to the unmodified hydrolysates, which had the crystal size of 47.2 μm (ZH) and 45.4 μm (GH). Also, the two succinylated samples had altered surface hydrophobicity, which potentially contributed to their enhanced IRI activity. Our results indicate that succinylation of food-derived protein hydrolysates can improve their IRI activity.

摘要

本研究旨在通过琥珀酰化修饰来提高玉米醇溶蛋白和明胶水解物(分别为 ZH 和 GH)的抗冰晶重结晶(IRI)活性。ZH 通过碱性蛋白酶处理 3 小时制备,然后用琥珀酸酐(SA)修饰;而 GH 则通过碱性蛋白酶水解 0.25 小时,并用正辛基琥珀酸酐(OSA)酰化。在 -8°C 下退火 0.5 小时,浓度为 40mg/mL 时,与未修饰的水解物相比,修饰后的水解物将冰晶的平均 Feret 直径从 50.2μm(聚乙二醇,阴性对照)降低至 28.8μm(SA 修饰的 ZH)和 29.5μm(OSA 修饰的 GH),而 ZH 和 GH 的原始晶体尺寸分别为 47.2μm 和 45.4μm。此外,这两种琥珀酰化样品的表面疏水性发生了改变,这可能有助于提高它们的抗冰晶重结晶活性。我们的结果表明,对食品来源的蛋白质水解物进行琥珀酰化修饰可以提高其抗冰晶重结晶活性。

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