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

BACKGROUND: This 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. METHOD: The 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. RESULTS: The 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. CONCLUSION: The molecular structural features related to protein biopolymer were highly associated with protein utilization and metabolism. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1186/s40104-019-0384-z) contains supplementary material, which is available to authorized users.