4.7 Article

Characterization of Endogenous Nanoparticles from Roasted Chicken Breasts

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 66, Issue 28, Pages 7522-7530

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.8b01988

Keywords

roasted chicken breasts; fluorescent nanoparticles; human serum albumin; thermodynamics; food thermal processing

Funding

  1. National Key Research and Development Program of China [2017YFD0400103, 2016YFD0400404]

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Emergence of endogenous nanoparticles in thermally processed food has aroused much attention due to their unique properties and potential biological impact. The aim of this study was to investigate the presence of fluorescence nanoparticles in roasted chicken breasts, elemental composition, physicochemical properties, and their molecular interaction with human serum albumin (HSA). Transmission electron microscopy analysis revealed that the foodborne nanoparticles from roasted chicken were nearly spherical with an average particle size of 1.7 +/- 0.4 nm. The elemental analysis of X-ray photoelectron spectroscopy showed the composition of nanoparticles as 47.4% C, 25.8% O, and 26.1% N. The fluorescence of HSA was quenched by the nanoparticles following a static mode, and the molecular interaction of nanoparticles with HSA was spontaneous (Delta G(0) < 0), where hydrogen bonding and van der Waals forces played an important role during HSA-nanoparticles complex stabilization through thermodynamic analysis by isothermal titration calorimetry. The principal location of the nanoparticles binding site on HSA was primarily in site I as determined by site-specific marker competition. The conformational of HSA was also changed and alpha-helical structure decreased in the presence of nanoparticles. Our studies revealed that fluorescent nanoparticles were produced after roasting of chicken breast at 230 C for 30 min for the first time. The obtained nanoparticles can interact with HSA in a spontaneous manner, thus providing valuable insight into foodborne NPs as well as their effects to human albumin protein.

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