Interactive association between processing induced molecular structure changes and nutrient delivery on a molecular basis, revealed by cutting-edge vibrational biomolecular spectroscopy

Abstract

BackgroundThis study was conducted to determine protein molecular structure profiles and quantify the relationship between protein structural features and protein metabolism and bioavailability of blend pelleted products (BPP) based on co-products (canola or carinata) from processing with different proportions of pulse pea screenings and lignosulfonate chemical compound.MethodThe protein molecular structures were determined using the non-invasive advanced vibrational molecular spectroscopy (ATR-FT/IR) in terms of chemical structure and biofunctional groups of amides (I and II), α-helix and β-sheet.ResultsThe results showed that increasing the level of the co-products in BPP significantly increased the spectral intensity of the amide area and amide height. The products exhibited similar protein secondary α-helix to β-sheet ratio. The protein molecular structure profiles (amides I and II, α-helix to β-sheet) were highly associated with protein degradation kinetics and intestinal digestion. In conclusion, the non-invasive vibrational molecular spectroscopy (ATR-FT/IR) could be used to detect inherent structural make-up characteristics in BPP.ConclusionThe molecular structural features related to protein biopolymer were highly associated with protein utilization and metabolism.Electronic supplementary materialThe online version of this article (10.1186/s40104-019-0384-z) contains supplementary material, which is available to authorized users.

Effect of carnosine synthesis precursors in the diet on jejunal metabolomic profiling and biochemical compounds in slow-growing Korat chicken

“…Previous studies ( Yu and Nuez-Ortín, 2010 ) indicate that the amide I to amide II ratio has a positive correlation with the metabolizable protein, while the slowly degradable fraction of protein is positively correlated with the amide I level. The amide I band, which is sensitive to small differentiation in molecular structure and hydrogen bonding motifs, is important for determining protein structural and conformational changes ( Ismael et al, 2019 ). Therefore, it is possible that the group of β-alanine precursor may affect amide I protein transformation because amide I can provide information on the vibrational bands of the protein backbone ( Sadat and Joye, 2020 ).…”