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Plant‐based food and feed protein structure changes induced by gene‐transformation, heating and bio‐ethanol processing: A synchrotron‐based molecular structure and nutrition research program
Author(s) -
Yu Peiqiang
Publication year - 2010
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.201000178
Subject(s) - synchrotron , synchrotron radiation , fourier transform , fourier transform infrared spectroscopy , beamline , infrared , transformation (genetics) , chemistry , brightness , biological system , materials science , nanotechnology , optics , physics , biology , gene , biochemistry , beam (structure) , quantum mechanics
Unlike traditional “wet” analytical methods which during processing for analysis often result in destruction or alteration of the intrinsic protein structures, advanced synchrotron radiation‐based Fourier transform infrared microspectroscopy has been developed as a rapid and nondestructive and bioanalytical technique. This cutting‐edge synchrotron‐based bioanalytical technology, taking advantages of synchrotron light brightness (million times brighter than sun), is capable of exploring the molecular chemistry or structure of a biological tissue without destruction inherent structures at ultra‐spatial resolutions. In this article, a novel approach is introduced to show the potential of the advanced synchrotron‐based analytical technology, which can be used to study plant‐based food or feed protein molecular structure in relation to nutrient utilization and availability. Recent progress was reported on using synchrotron‐based bioanalytical technique synchrotron radiation‐based Fourier transform infrared microspectroscopy and diffused reflectance infrared Fourier transform spectroscopy to detect the effects of gene‐transformation (Application 1), autoclaving (Application 2), and bio‐ethanol processing (Application 3) on plant‐based food and feed protein structure changes on a molecular basis. The synchrotron‐based technology provides a new approach for plant‐based protein structure research at ultra‐spatial resolutions at cellular and molecular levels.