Development and refurbishment of energy-efficient residential districts based on collective self-organised housing processes
Bibliographic record
Abstract
This study aimed to investigate the biological potential of underutilized and low-value corn distillers solubles, containing a unique unexplored blend of heat-treated corn and yeast proteins, from the bioethanol industries, by bioinformatic and biochemical approaches. Protein hydrolysates were produced by applying four commercially accessible proteases, among which alcalase provided the best results in terms of yield, degree of hydrolysis, molecular weight, number of proteins, bioactive peptides, and deactivation against anti-angiotensin I-converting enzyme (ACE) and anti-dipeptidyl peptidase IV (DPP IV). The optimal conditions to produce anti-ACE and anti-DPP IV peptides were using alcalase for 10.82 h and an enzyme : substrate ratio of 7.90 (%w/w), with inhibition values for ACE and DPP IV of 98.76 ± 1.28% and 34.99 ± 1.44%, respectively. Corn (α-zein) and yeast (glyceraldehyde-3-phosphate dehydrogenase) proteins were mainly suitable, upon enzymolysis, for the release of bioactive peptides. The peptides DPANLPWG, FDFFDNIN, WNGPPGVF, and TPPFHLPPP inhibited ACE more effectively as verified with binding energies of -11.3, -11.6, -10.5, and -11.6 kcal mol<sup>-1</sup>, respectively, as compared to captopril (-6.38 kcal mol<sup>-1</sup>). Compared with the binding energy of sitagliptin (-8.6 kcal mol<sup>-1</sup>), WNGPPGVF (-9.6 kcal mol<sup>-1</sup>), WPLPPFG (-9.8 kcal mol<sup>-1</sup>), LPPYLPS (-9.7 kcal mol<sup>-1</sup>), TPPFHLPPP (-10.1 kcal mol<sup>-1</sup>), and DPANLPWG peptides (-10.1 kcal mol<sup>-1</sup>) had greater inhibition potential against DPP IV. The peptides impeded ACE and DPP IV majorly <i>via</i> hydrophobic and hydrogen linkage interactions. The key amino acids TYR<sup>523</sup>, GLU<sup>384</sup>, and HIS<sup>353</sup> were bound to the catalytic sites of ACE and GLN<sup>553</sup>, GLU<sup>206</sup>, PHE<sup>364</sup>, VAL<sup>303</sup>, and THR<sup>304</sup> were bound to the DPP IV enzyme. The PHs can be used as ingredients in the feed or food industries with possible health advantages.
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How this classification was reachedexpand
Full frame machine prediction
Teacher imitationNot calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.
Distilled classifier scores by category (both heads)
| Category | Codex | Gemma |
|---|---|---|
| Metaresearch | 0.000 | 0.000 |
| Meta-epidemiology (narrow) | 0.000 | 0.000 |
| Meta-epidemiology (broad) | 0.000 | 0.000 |
| Bibliometrics | 0.000 | 0.000 |
| Science and technology studies | 0.000 | 0.000 |
| Scholarly communication | 0.000 | 0.000 |
| Open science | 0.001 | 0.001 |
| Research integrity | 0.000 | 0.000 |
| Insufficient payload (model declined to judge) | 0.001 | 0.001 |
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 itClassification
machine, unvalidatedMachine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.
How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".