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.

Highlights

  • 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 from processing with different proportions of pulse pea screenings and lignosulfonate chemical compound

  • The results showed that BPP7 and BPP3 had the highest (P < 0.01) amide I peak height, while the BPP2 and

  • Our results showed that the ratio of amide I to amide II was higher (P < 0.05) in BPP based on the new co-product of carinata meal compared with coproduct of canola meal (2.12 vs. 1.98)

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Summary

Introduction

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. The current study was performed to 1) investigate the differences among eight blend pellet products (BPP) from the bio-energy processing (new carinata meal vs canola meal) with different proportions of pea screenings and lignosulfonate compound in terms of protein molecular structure; and 2) to quantify the protein inherent molecular structure changes in relation to protein profile, Cornell Net Carbohydrate, and Protein System (CNCPS) protein subfractions, energy values, protein digestion (rumen and intestine), and the metabolizable protein supply. The hypothesis of this study was that vibrational Fourier transform infrared spectroscopy could be used to detect an interactive association of processing induced molecule structural changes in biofunctional groups of protein amides I and II, alpha-helix and beta-sheet in the BPPs with protein metabolism and utilization

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