Journal of Food Science and Biotechnology
Abstract
[Objective ] This study aims to design a fusion protein with high activities and high stability of superoxide dismutase (SOD ) and catalase (CAT ).[Method ] Using AcSOD 11 and FeCAT proteins as the research subjects,three fusion proteins of SOD and CAT were designed:AcSOD 11-(GGGGS )*3-FeCAT,FeCAT-(GGGGS )*3-AcSOD 11,and FeCAT- (EAAAK )*3-AcSOD 11,which were named AcSOD 11-G3-FeCAT,FeCAT-G3-AcSOD 11,and FeCAT-E 3-AcSOD 11,respectively.Soluble expression of these three fusion proteins was achieved in Escherichia coli BL21(DE3).The thermal stability and pH stability of the three fusion proteins were then assessed.[Result ] The three fusion proteins showed no significant difference in the specific activity of SOD,while they had significant differences in the specific activity of CAT.The specific activity of CAT was the highest (531 U/mg ) in FeCAT-G 3-AcSOD 11 and the lowest in FeCAT-E 3-AcSOD 11,indicating that the flexible (GGGGS )*3 peptide linker was favorable for maintaining CAT enzyme activity.Stress resistance studies demonstrated that both CAT and SOD in FeCAT-G 3-AcSOD 11 exhibited strong tolerance to high temperatures and varying pH conditions.[Conclusion ] This study successfully constructed three fusion proteins and obtained FeCAT-G 3-AcSOD 11,a highly stable fusion protein with high enzyme activities of both SOD and CAT,providing a theoretical foundation for the combined application of SOD and CAT.
Publication Date
12-15-2025
First Page
165
Last Page
172
DOI
10.12441/spyswjs.20241115002
Recommended Citation
JIANG, Zhuo; LU, Weina; LIN, Qi; LUO, Zhan; LYU, Zhengbin; and NIE, Zuoming
(2025)
"Design , Expression , and Stability Evaluation of a Superoxide Dismutase-catalase Fusion Protein,"
Journal of Food Science and Biotechnology: Vol. 44:
Iss.
12, Article 17.
DOI: 10.12441/spyswjs.20241115002
Available at:
https://spsw.spyswjs.cnjournals.com/journal/vol44/iss12/17
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