Abstract：
BACKGROUND: The increasing demand for sustainable alternatives to traditional protein sources, driven by population growth, underscores the importance of protein in a healthy diet. Pecan (Carya illinoinensis (Wangenh.) K. Koch) nuts are currently underutilized as plant-based proteins but hold great potential in the food industry. However, there is insufficient information available on pecan protein, particularly its protein fractions. This study aimed to explore the physicochemical and functional properties of protein isolate and the main protein fraction glutelin extracted from pecan nuts.
RESULTS: The results revealed that glutelin (820.67 ± 69.42 g kg-1) had a higher crude protein content compared to the protein isolate (618.43 ± 27.35 g kg-1), while both proteins exhibited amino acid profiles sufficient for adult requirements. The isoelectric points of protein isolate and glutelin were determined to be pH 4.0 and pH 5.0, respectively. The denaturation temperature of the protein isolate (90.23 °C) was higher than that of glutelin (87.43 °C), indicating a more organized and stable conformation. This is further supported by the fact that the protein isolate had a more stable main secondary structure than glutelin. Both proteins demonstrated improved solubility, emulsifying, and foaming properties at pH levels deviating from their isoelectric points in U-shaped curves. Compared to the protein isolate, glutelin displayed superior water and oil absorption capacity along with enhanced gelling ability.
CONCLUSIONS: The protein isolate and glutelin from pecan nuts exhibited improved stability and competitive functional properties, respectively. The appropriate utilization of these two proteins will support their potential as natural ingredients in various food systems. © 2024 Society of Chemical Industry.
RESULTS: The results revealed that glutelin (820.67 ± 69.42 g kg-1) had a higher crude protein content compared to the protein isolate (618.43 ± 27.35 g kg-1), while both proteins exhibited amino acid profiles sufficient for adult requirements. The isoelectric points of protein isolate and glutelin were determined to be pH 4.0 and pH 5.0, respectively. The denaturation temperature of the protein isolate (90.23 °C) was higher than that of glutelin (87.43 °C), indicating a more organized and stable conformation. This is further supported by the fact that the protein isolate had a more stable main secondary structure than glutelin. Both proteins demonstrated improved solubility, emulsifying, and foaming properties at pH levels deviating from their isoelectric points in U-shaped curves. Compared to the protein isolate, glutelin displayed superior water and oil absorption capacity along with enhanced gelling ability.
CONCLUSIONS: The protein isolate and glutelin from pecan nuts exhibited improved stability and competitive functional properties, respectively. The appropriate utilization of these two proteins will support their potential as natural ingredients in various food systems. © 2024 Society of Chemical Industry.
摘要：
背景：对传统蛋白质来源的可持续替代品的需求不断增加，在人口增长的推动下，强调蛋白质在健康饮食中的重要性。山核桃(美国山核桃(旺根。）K.Koch）坚果目前未被充分利用作为植物性蛋白质，但在食品工业中具有巨大潜力。然而,关于山核桃蛋白的信息不足，特别是它的蛋白质部分。本研究旨在探索从山核桃坚果中提取的分离蛋白和主要蛋白组分谷蛋白的理化性质和功能性质。
结果：结果表明，与分离蛋白（618.43±27.35gkg-1）相比，谷蛋白（820.67±69.42gkg-1）具有更高的粗蛋白含量，而两种蛋白质都表现出足以满足成人需求的氨基酸谱。分离蛋白和谷蛋白的等电点分别确定为pH4.0和pH5.0。分离蛋白的变性温度(90.23℃)高于谷蛋白的变性温度(87.43℃),表明更有组织和稳定的构象。蛋白分离物具有比谷蛋白更稳定的主要二级结构的事实进一步支持了这一点。两种蛋白质都表现出改善的溶解度，乳化,在pH值水平下的发泡性能偏离其等电点的U形曲线。与分离蛋白相比，谷蛋白显示出优异的水和油吸收能力以及增强的胶凝能力。
结论：来自山核桃的蛋白质分离物和谷蛋白显示出改善的稳定性和竞争性功能特性，分别。这两种蛋白质的适当利用将支持它们作为各种食物系统中的天然成分的潜力。©2024化学工业学会。
结果：结果表明，与分离蛋白（618.43±27.35gkg-1）相比，谷蛋白（820.67±69.42gkg-1）具有更高的粗蛋白含量，而两种蛋白质都表现出足以满足成人需求的氨基酸谱。分离蛋白和谷蛋白的等电点分别确定为pH4.0和pH5.0。分离蛋白的变性温度(90.23℃)高于谷蛋白的变性温度(87.43℃),表明更有组织和稳定的构象。蛋白分离物具有比谷蛋白更稳定的主要二级结构的事实进一步支持了这一点。两种蛋白质都表现出改善的溶解度，乳化,在pH值水平下的发泡性能偏离其等电点的U形曲线。与分离蛋白相比，谷蛋白显示出优异的水和油吸收能力以及增强的胶凝能力。
结论：来自山核桃的蛋白质分离物和谷蛋白显示出改善的稳定性和竞争性功能特性，分别。这两种蛋白质的适当利用将支持它们作为各种食物系统中的天然成分的潜力。©2024化学工业学会。
