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

Abstract

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.

SR-IMS Molecular Spectroscopic Image of Functional Groups in Biopolymers in Feed Systems

“…These bands are highly associated mainly with lipid and minor with protein (15). The embryo tissue also contains high amide I and amide II bands (2,8,9), indicated high protein composition in the embryo. From the pixel spectra pattern, it was found that sorghum embryo contains relatively high protein beta-sheet (ca.…”

“…It is a very unique from visible image. However, the detailed chemistry of embryo tissue in its original form in sorghum seed is not fully understood due to limited analytical technique available before available synchrotron-based technique (2). The photomicrographs of the tissue are not informative with respect to molecular chemical features of the inherent structures at spatial resolution (6).…”

“…This technique enables to collect the spectral data at the diffraction limit or a few microns without destruction of inherent tissue structure (1,3,4), which is not possible to use previous techniques. 2 and CH 3 anti-symmetric and symmetric stretching bands at the region of ca. 2990-2780 cm -1 , amide I and II bands at ca.…”

“…The amide II (predominantly an N-H bending vibration coupled to C-N s t r e t c h i n g ) i s a l s o u s e d t o a s s e s s p r o t e i n c o n f o r m a t i o n . H o w e v e r , a s i t a r i s e s f r o m complex vibrations involving multiple functional groups, it is less useful for protein structure prediction than the amide I (2,8,9). No any publication has been found to map the embryo tissue in the literature.…”

“…This size was within cellular dimension and was the best for getting good signal to noise ratio spectrum mapping in complex plant system. To minimize IR absorption by CO 2 and water vapour in ambient air, the optics were purged using dry N 2 . A background spectroscopic image file was collected from an area free of sample.…”