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 pel eted prod...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 pel eted 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(ⅠandⅡ),α-helix andβ-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 secondaryα-helix toβ-sheet ratio.The protein molecular structure profiles(amidesⅠandⅡ,α-helix toβ-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.展开更多
基金financially supported by the grants from Sask Pulse Growers,Natural Sciences and Engineering Research Council of Canada(NSERC)the Sask Canola,the Ministry of Agriculture Strategic Research Chair ProgramSask Milk.
文摘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 pel eted 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(ⅠandⅡ),α-helix andβ-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 secondaryα-helix toβ-sheet ratio.The protein molecular structure profiles(amidesⅠandⅡ,α-helix toβ-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.
