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

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.