title: Dispersible and thermal stable nanofibrils derived from glycated whey protein.
abstract: Formation of nanofibrils by heating proteins at pH 2.0 has been studied extensively because of the potential as novel biomaterials. However, nanofibrils of whey proteins have poor dispersibility and heat stability, limiting their application in fluidic and transparent products. We report, for the first time, the formation of nanofibrils from whey protein isolate (WPI) glycated with lactose (WPI-g-L) that were highly dispersible and remained transparent after heating at pH 3.0-7.0 and 0-150 mM NaCl. The WPI-g-L followed similar nanofibril formation mechanism as WPI based on reducing protein electrophoresis, analytical ultracentrifugation, and circular dichroism spectroscopy. The rate of nanofibril formation from WPI-g-L was similar to that of WPI, but the yield was lower based on thioflavin-T fluorescence spectroscopy. The presence of the glycated lactose on nanofibril surface provided steric hindrance enabling the dispersibility and thermal stability and supplying functions such as viscosity in various fluidic, transparent consumer products.
authors.affiliation: Department of Food Science and Technology, The University of Tennessee, Knoxville, Tennessee, United States.
authors.forename: Gang
authors.initials: G
authors.lastname: Liu
authors.forename: Qixin
authors.initials: Q
authors.lastname: Zhong
mesh_terms: D006031:Glycosylation; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D007785:Lactose / Q000737:chemistry; D018625:Microscopy, Atomic Force; D046529:Microscopy, Electron, Transmission; D008894:Milk Proteins / Q000737:chemistry*; D057139:Nanofibers / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014783:Viscosity; D000067816:Whey Proteins
chemical_list: D008894:Milk Proteins; D000067816:Whey Proteins; D007785:Lactose