Affiliations 

  • 1 Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi214000, Jiangsu, China
  • 2 Nanjing Medical University , 140 Hanzhong Road, Nanjing210029, China
  • 3 Department of Food Science and Nutrition, Faculty of Agriculture, Sana'a University, Sana'a0000, Yemen
  • 4 Laboratory of Food Safety and Food Integrity, Universiti Putra Malaysia (UPM), 43400 UPMSerdang, Selangor, Malaysia
  • 5 School of Chemistry and Chemical Engineering, Guangxi University, Nanning530004, Guangxi, China
J Agric Food Chem, 2026 Oct 28;74(42):33165-33183.
PMID: 42949349 DOI: 10.1021/acs.jafc.6c10478

Abstract

Cu/Zn superoxide dismutase (Cu/Zn-SOD) is a key antioxidant enzyme that catalyzes superoxide radical dismutation. Here, an integrated computational-assisted, structure-guided engineering strategy was applied to improve Cu/Zn-SOD catalytic performance. Gln22 and Glu134 were identified as promising engineering sites, and saturation mutagenesis yielded Q22I and E134 M as the most beneficial single substitutions, with specific activities 1.55- and 2.39-fold higher than wild type (WT), respectively. Combining both substitutions generated M2 (Q22I/E134M), which showed the highest specific activity of 7121.0 U mg-1, corresponding to a 3.43-fold increase over WT. The optimal temperature of Q22I and M2 increased from 40 to 50 °C, and M2 also exhibited enhanced thermostability. Kinetic analysis showed that M2 had a 41.18% lower Km and a 2.95-fold higher Vmax than WT. Molecular docking suggested complementary effects of Q22I and E134 M on structural stability and active-site optimization, supporting improved catalytic performance. These findings provide a basis for engineering efficient, thermostable SODs.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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