| Authors: |
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. |
| Abstract: |
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 ΔGbind became 98.98% more negative, matching the experimental 99.36-fold reduction in Kcat/Km. In summary, IPF at 130 °C-9 min effectively inactivated urease via significant disruption of conformational structures and catalytic function. |