Rational Design of Disulfide Bonds for Increasing the Activity and Stability of Penicillium verruculosum Polysaccharide Monooxygenase
Abstract Rational design of disulfide bonds in P. verruculosum polysaccharide monooxygenase was carried out. It was shown that the increase in enzyme activity and thermostability correlates with the location of the disulfide bond in the region of a highly mobile loop near the active center in the three-dimensional structure of the enzyme. It was also demonstrated that thermal denaturation of P. verruculosum polysaccharide monooxygenase is reversible and the enzyme fully restores activity after incubation at 4°C.
Authors
- А. М. Рожкова (ORCID: https://orcid.org/0000-0003-4901-4705)
- Ekaterina A. Rubtsova
- Ivan N. Zorov (ORCID: https://orcid.org/0000-0001-6888-172X)
- Olga A. Sinitsyna (ORCID: https://orcid.org/0000-0001-5424-7402)
- Arkadiy P. Sinitsyn (ORCID: https://orcid.org/0000-0001-6234-5395)
- Sergei A. Kurzeev (ORCID: https://orcid.org/0000-0002-0016-8036)
- A. S. Dotsenko
Institutions
- Russian Academy of Sciences (RU)
- Lomonosov Moscow State University (RU)
- Federal Research Centre «Fundamentals of Biotechnology» of the Russian Academy of Sciences (RU)
Publication Details
- Journal
- Moscow University Chemistry Bulletin
- Published
- 2026-10-26
- DOI
- https://doi.org/10.3103/s0027131426700288
- Primary Topic
- Enzyme Catalysis and Immobilization
- Type
- article
- Field-Weighted Citation Impact
- 0.00