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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/41922
Title: Improving enzymatic activities and thermostability of a tri-functional enzyme with SOD, catalase and cell-permeable activities
Authors: Piriya Luangwattananun
Warawan Eiamphungporn
Napat Songtawee
Leif Bülow
Chartchalerm Isarankura Na Ayudhya
Virapong Prachayasittikul
Sakda Yainoy
Mahidol University
Lunds Universitet
Keywords: Biochemistry, Genetics and Molecular Biology;Chemical Engineering;Immunology and Microbiology
Issue Date: 10-Apr-2017
Citation: Journal of Biotechnology. Vol.247, (2017), 50-59
Abstract: © 2017 Elsevier B.V. Synergistic action of major antioxidant enzymes, e.g., superoxide dismutase (SOD), catalase (CAT) and glutathione peroxidase (GPx) is known to be more effective than the action of any single enzyme. Recently, we have engineered a tri-functional enzyme, 6His-MnSOD-TAT/CAT-MnSOD (M-TAT/CM), with SOD, CAT and cell-permeable activities. The protein actively internalized into the cells and showed superior protection against oxidative stress-induced cell death over native enzymes fused with TAT. To improve its molecular size, enzymatic activity and stability, in this study, MnSOD portions of the engineered protein were replaced by CuZnSOD, which is the smallest and the most heat resistant SOD isoform. The newly engineered protein, CAT-CuZnSOD/6His-CuZnSOD-TAT (CS/S-TAT), had a 42% reduction in molecular size and an increase in SOD and CAT activities by 22% and 99%, respectively. After incubation at 70 °C for 10 min, the CS/S-TAT retained residual SOD activity up to 54% while SOD activity of the M-TAT/CM was completely abolished. Moreover, the protein exhibited a 5-fold improvement in half-life at 70 °C. Thus, this work provides insights into the design and synthesis of a smaller but much more stable multifunctional antioxidant enzyme with ability to enter mammalian cells for further application as protective/therapeutic agent against oxidative stress-related conditions.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85014883108&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/41922
ISSN: 18734863
01681656
Appears in Collections:Scopus 2016-2017

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