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静电纺丝马铃薯蛋白-麦芽糊精混合物及热糖基化对胰蛋白酶抑制剂活性的影响

Effects of Electrospun Potato Protein-Maltodextrin Mixtures and Thermal Glycation on Trypsin Inhibitor Activity.

作者信息

Gibis Monika, Pribek Franziska, Weiss Jochen

机构信息

Department of Food Material Science, Institute of Food Science and Biotechnology, University of Hohenheim, Garbenstr. 25, 70599 Stuttgart, Germany.

出版信息

Foods. 2022 Mar 23;11(7):918. doi: 10.3390/foods11070918.

DOI:10.3390/foods11070918
PMID:35407004
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8997613/
Abstract

Fibers of potato protein and polysaccharides were obtained by needleless electrospinning. Mixtures of maltodextrin DE2 (dextrose equivalent) (0.8 g/mL), DE21 (0.1 g/mL), and different concentrations of potato protein (0.05, 0.1, 0.15, and 0.2 g/mL) were used for fiber production. Glycation was performed via the Maillard reaction after thermal treatment (0/6/12/24/48 h, 65 °C, 75% relative humidity). The effects of electrospinning and heating on trypsin inhibitor activity (IA) were studied. The results of the IA assay showed that electrospinning and glycation caused significant differences in IA among blends, heating times, and the interaction of blend and heating time (p < 0.001). The higher the protein content in the fibers, the higher the IA. The lowest IA was found in the mixture with the lowest protein content after 48 h. In other blends, the minimum IAs were found between 6 and 12 h of heating. The determination of the free lysine groups showed a nonsignificant decrease after heating. However, higher free lysine groups per protein (6.3−9.5 g/100 g) were found in unheated fibers than in the potato protein isolate (6.0 ± 0.5 g/100 g). The amide I and amide II regions, detected by the Fourier transform infrared spectra, showed only a slight shift after heating.

摘要

通过无针静电纺丝获得了马铃薯蛋白和多糖纤维。使用麦芽糊精DE2(葡萄糖当量)(0.8 g/mL)、DE21(0.1 g/mL)与不同浓度的马铃薯蛋白(0.05、0.1、0.15和0.2 g/mL)的混合物来生产纤维。在热处理(0/6/12/24/48小时,65°C,75%相对湿度)后通过美拉德反应进行糖基化。研究了静电纺丝和加热对胰蛋白酶抑制活性(IA)的影响。IA测定结果表明,静电纺丝和糖基化在共混物、加热时间以及共混物与加热时间的相互作用之间导致IA存在显著差异(p < 0.001)。纤维中蛋白质含量越高,IA越高。在48小时后,蛋白质含量最低的混合物中IA最低。在其他共混物中,在加热6至12小时之间发现了最低的IA。游离赖氨酸基团的测定显示加热后有不显著的减少。然而,未加热的纤维中每克蛋白质的游离赖氨酸基团含量(6.3−9.5 g/100 g)高于马铃薯分离蛋白(6.0±0.5 g/100 g)。通过傅里叶变换红外光谱检测的酰胺I和酰胺II区域在加热后仅显示出轻微的位移。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6ce/8997613/2371e8d8b113/foods-11-00918-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6ce/8997613/7927bbe1f836/foods-11-00918-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6ce/8997613/7ce4abe448a4/foods-11-00918-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6ce/8997613/89349ad663f0/foods-11-00918-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6ce/8997613/3c339d7543b7/foods-11-00918-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6ce/8997613/2371e8d8b113/foods-11-00918-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6ce/8997613/7927bbe1f836/foods-11-00918-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6ce/8997613/7ce4abe448a4/foods-11-00918-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6ce/8997613/89349ad663f0/foods-11-00918-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6ce/8997613/3c339d7543b7/foods-11-00918-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6ce/8997613/2371e8d8b113/foods-11-00918-g005.jpg

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