Formation and Physicochemical Properties of Freeze-Dried Amyloid-Like Fibrils From Pinto Bean Protein: Amyloid-Like Fibrils From Pinto Bean Protein.

IF 1.5 4区 化学 Q3 CHEMISTRY, ANALYTICAL International Journal of Analytical Chemistry Pub Date : 2024-10-23 eCollection Date: 2024-01-01 DOI:10.1155/2024/5571705
Ameneh Allameh, Mohammad Fazel, Nafisehsadat Sheikhan, Mohammad Goli
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Abstract

Amyloid nanofibrils are long and thin strands with cross β structures associated by hydrogen bonds. These structures can be formed under suitable conditions commonly at low pH and high temperatures. Fibrillated pinto bean protein isolate (FPBPI) was made by heating pinto bean protein at 85°C in an acidic condition while gently stirring at initial protein solution concentrations of 4 mg/mL, 13 mg/mL, and 21 mg/mL. Freeze-dried FPBPI's physicochemical, structural, and thermal characteristics were assessed, and they were compared with a native pinto bean protein isolate (PBPI) as a control. An increase in Congo red spectral absorption at 544 nm was observed following the fibril formation process. The largest concentration of freeze-dried fibrillated protein exhibited the highest Congo red spectral absorption. Fibrillar proteins' Fourier transform infrared (FTIR) spectrograms with lower wave numbers were seen than the native protein. For native PBPI, transmission electron microscopy (TEM) images were globular in shape, but they changed to long and curly morphologies in fibrillated proteins. FPBPI has a lower melting enthalpy than native protein when measured by differential scanning calorimetry (DSC). With the rising initial protein content, the enthalpy rose. Concurrently, semicrystalline structure for native and fibrillated pinto bean proteins was revealed by X-ray diffraction (XRD) findings. As the original protein concentration grew, so did the crystallinity intensity. Water-holding capacity (WHC) and oil-holding capacity (OHC) of freeze-dried FPBPI were higher than those of native protein. So, fibrillation of pinto bean protein helped it to serve as a good thickener in food industries.

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冷冻干燥松豆蛋白淀粉样纤维的形成与理化性质:松豆蛋白中的淀粉样纤维。
淀粉样蛋白纳米纤维是由氢键连接的具有交叉 β 结构的细长股。这些结构可在适当的条件下形成,通常是在低 pH 值和高温条件下。纤丝松豆蛋白分离物(FPBPI)是在酸性条件下于 85°C 加热松豆蛋白,同时轻轻搅拌,初始蛋白溶液浓度分别为 4 毫克/毫升、13 毫克/毫升和 21 毫克/毫升。对冷冻干燥的 FPBPI 的理化、结构和热特性进行了评估,并与作为对照的原生松豆蛋白分离物(PBPI)进行了比较。纤维形成后,在 544 纳米波长处观察到刚果红光谱吸收增加。最大浓度的冻干纤维化蛋白质表现出最高的刚果红光谱吸收率。纤维蛋白质的傅立叶变换红外光谱图的波数低于原生蛋白质。原生 PBPI 的透射电子显微镜(TEM)图像呈球状,而纤维化蛋白质的图像则变为长卷状。用差示扫描量热法(DSC)测量,FPBPI 的熔化焓低于原生蛋白质。随着初始蛋白质含量的增加,熔化焓也随之升高。同时,X 射线衍射(XRD)结果显示,原生蛋白和纤维化松豆蛋白具有半晶体结构。随着原始蛋白质浓度的增加,结晶度也在增加。冷冻干燥后的原生蛋白的持水量(WHC)和持油量(OHC)均高于原生蛋白。因此,松豆蛋白的纤维化有助于其在食品工业中成为一种良好的增稠剂。
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来源期刊
CiteScore
3.10
自引率
5.60%
发文量
117
期刊介绍: International Journal of Analytical Chemistry publishes original research articles that report new experimental results and methods, especially in relation to important analytes, difficult matrices, and topical samples. Investigations may be fundamental, or else related to specific applications; examples being biological, environmental and food testing, and analysis in chemical synthesis and materials processing. As well as original research, the International Journal of Analytical Chemistry also publishes focused review articles that examine the state of the art, identify emerging trends, and suggest future directions for developing fields.
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Formation and Physicochemical Properties of Freeze-Dried Amyloid-Like Fibrils From Pinto Bean Protein: Amyloid-Like Fibrils From Pinto Bean Protein. Prediction of Lycii Cortex Quality Marker Based on Network Pharmacology and Chemometrics Methods. Determination of Alzheimer's Drugs in a Human Urine Sample by Different Chemometric Methods: Chemometric Determination of Alzheimer's Drugs. Development of the Pipette-Tip Micro-Solid-Phase Extraction for Extraction of Rutin From Moringa oleifera Lam. Using Activated Hollow Carbon Nanospheres as Sorbents. Establishment of a Generalizable Industrial Crop Model for Microwave Extraction of Unsaturated Fatty Acids.
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