Structural changes on a molecular basis of canola meal by conditioning temperature and time during pelleting process in relation to physiochemical (energy and protein) properties relevant to ruminants

The objectives of this study were: (1) To investigate the effects of conditioning temperature (70, 80, 90°C), time (30, 60 sec), and interaction (temperature × time) during the pelleting process on internal protein molecular structure changes of the co-products; (2) To identify differences in protein molecular structures among pellets that were processed under different conditions, and between unprocessed mash and pellets; 3) To quantify protein molecular structure changes in relation to predicted energy and protein utilization in dairy cows. The final goal of this program was to show how processing conditions changed internal feed structure on a molecular basis and how molecular structure changes induced by feed processing affected feed milk value in dairy cows. The hypothesis in this study was that processing-induced protein inherent structure changes affected energy and protein availability in dairy cattle and the sensitivity and response of protein internal structure to the different pelleting process conditions could be detected by advanced molecular spectroscopy. The protein molecular structures, amides I and II, amide I to II ratios, α-helix structure, β-sheet structure, and α to β structure ratios, were determined using the advanced vibrational molecular spectroscopy (ATR-FT/IR). The energy values were determined using NRC2001 summary approach in terms of total digestible nutrients, metabolizable and net energy for lactation. The protein and carbohydrate subfactions that are related to rumen degradation characteristics and rumen undegraded protein supply were determined using updated CNCPS system. The experiment design was a RCBD and the treatment design was a 3x2 factorial design. The results showed that pelleting induced changes in protein molecular structure. The sensitivity and response of protein inherent structure to the pelleting depended on the conditioning temperature and time. The protein molecular structure changes were correlated (P