Academic Journal
Unraveling Structural Changes and the Reaction Mechanism in Urease upon Infrared Physical Inactivation.
| Τίτλος: | Unraveling Structural Changes and the Reaction Mechanism in Urease upon Infrared Physical Inactivation. |
|---|---|
| Συγγραφείς: | Shen T; School of Food Science and Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang, Jiangsu 212013, PR China., Liu Y; School of Food Science and Engineering, Chongqing Technology and Business University, 19 Xuefu Avenue, Nan'an District, Chongqing 400010, PR China., Qu W; School of Food Science and Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang, Jiangsu 212013, PR China.; Institute of Food Physical Processing, Jiangsu University, 301 Xuefu Road, Zhenjiang, Jiangsu 212013, PR China., Ma H; School of Food Science and Engineering, Jiangsu University, 301 Xuefu Road, Zhenjiang, Jiangsu 212013, PR China.; Institute of Food Physical Processing, Jiangsu University, 301 Xuefu Road, Zhenjiang, Jiangsu 212013, PR China., Jiang Q; Zhenjiang Meibo Infrared Technology Co., Ltd, Dingmao Technology New Town, Zhenjiang, Jiangsu 212013, PR China., Huang Y; Taizhou Agricultural Machinery Technology Promotion Station, Taizhou, Jiangsu 225300, PR China. |
| Πηγή: | Journal of agricultural and food chemistry [J Agric Food Chem] 2026 Jul 22; Vol. 74 (28), pp. 22172-22186. Date of Electronic Publication: 2026 Jul 09. |
| Τύπος έκδοσης: | Journal Article |
| Γλώσσα: | English |
| Στοιχεία περιοδικού: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 0374755 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5118 (Electronic) Linking ISSN: 00218561 NLM ISO Abbreviation: J Agric Food Chem Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: Washington, American Chemical Society. |
| Ιατρικοί όροι (MeSH): | Urease*/chemistry , Urease*/metabolism, Protein Conformation/radiation effects ; Kinetics ; Hydrophobic and Hydrophilic Interactions ; Molecular Dynamics Simulation ; Infrared Rays ; Hydrogen Bonding ; Hot Temperature |
| Περίληψη: | To improve energy efficiency and inhibit urease, this study developed an infrared physical field (IPF) method. This study integrates experimental approaches and computational simulations to elucidate the mechanism of urease inactivation under IPF treatment. The optimal treatment (130 °C-9 min) reduced the enzyme activity by 97.55% within the experimental range (90-130 °C, 1-9 min). Experimentally, circular dichroism showed a 25.36% increase in random coil content, and hydrophobicity assays showed a 1.23-fold increase in surface hydrophobicity. Molecular dynamics simulations predicted disruption of intra- and intermolecular hydrogen bonds (2.60% and 11.69%), van der Waals interactions (99.99%), and electrostatic interactions (96.80%). The computed ΔG |
| Contributed Indexing: | Keywords: binding energy calculation; enzyme structural response; infrared physical field; molecular dynamics/docking; urease inhibition mechanism |
| Substance Nomenclature: | EC 3.5.1.5 (Urease) |
| Entry Date(s): | Date Created: 20260709 Date Completed: 20260722 Latest Revision: 20260722 |
| Update Code: | 20260722 |
| DOI: | 10.1021/acs.jafc.6c02294 |
| PMID: | 42424503 |
| Βάση Δεδομένων: | MEDLINE |
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