Vibrational spectroscopic investigation of heat-induced changes in functional groups related to protein structural conformation in camelina seeds and their relationship to digestion in dairy cows
Why this work is in the frame
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Bibliographic record
Abstract
The objective of this study was to use Fourier transform/infrared-attenuated total reflectance (FT/IR-ATR) molecular spectroscopy to quantify the heat-induced changes in feed protein molecular structures in relation to protein digestion in dairy cows. Camelina seeds were evaluated in this study as a model for feed protein. The seeds were either heated in air-draft oven (dry heating) or in autoclave (moist heating) at 120°C for 60 min or kept as raw (control). The parameters evaluated were Cornell net protein and carbohydrate system (CNCPS) subfractions, in situ ruminal degradation kinetics, intestinal digestibility of rumen undegraded protein (RUP) and protein molecular structures. Moist heating decreased (P < 0.05) the content of total rumen degradable (RDP) crude protein (CP) subfractions and increased the content of total RUP subfractions compared with raw seeds, indicating a significant shift at the site of protein digestion from rumen to post-ruminal tract. The decrease in RDP was mainly related to the marked decrease in rapidly solubilised (PA) and degradable (PB1) fractions, whereas the moderately degradable (PB2) and slowly degradable (PB3) fractions increased, suggesting a decrease in degradation rate of RDP. The in situ rumen incubation study revealed that moist heating decreased (P < 0.05) RDP and increased (P < 0.05) RUP and its intestinal digestibility. The molecular spectroscopy study revealed that moist heating altered protein molecular structures. Except PA and lag time, dry heating did not significantly alter any of the CNCPS CP subfraction, in situ ruminal CP degradation parameters, intestinal digestibility of RUP, and protein molecular structures. The correlation analysis showed that the heat-induced changes in protein secondary structures, a-helix-to-ß-sheet ratio, were positively correlated (P < 0.05) with the contents PA (r = 0.90), PB1 (r = 0.89), RDP (r = 0.72) and intestinal digestibility (r = 0.91) of RUP, and negatively correlated (P < 0.05) with PB2 (r = –0.90), PB3 (r = –0.85) and RUP (–0.87). These results showed that compared with dry heating, moist heating significantly changed protein subfractions, rumen degradability and intestinal digestibility, and these changes were strongly associated with changes in protein molecular structures.
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Full frame distilled prediction
Teacher imitationNot calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.
Codex and Gemma teacher scores by category
| Category | Codex | Gemma |
|---|---|---|
| Metaresearch | 0.001 | 0.001 |
| Meta-epidemiology (narrow) | 0.000 | 0.000 |
| Meta-epidemiology (broad) | 0.000 | 0.000 |
| Bibliometrics | 0.000 | 0.002 |
| Science and technology studies | 0.000 | 0.000 |
| Scholarly communication | 0.000 | 0.001 |
| Open science | 0.000 | 0.000 |
| Research integrity | 0.000 | 0.000 |
| Insufficient payload (model declined to judge) | 0.000 | 0.000 |
Machine scores (provisional)
The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.
Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.
score_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it