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CAP modifies the structure of a model protein from thermophilic bacteria: mechanisms of CAP-mediated inactivation

Pankaj AttriResearch Group PLASMANT, Department of Chemistry, University of Antwerp, Universiteitsplein 1, B-2610, Antwerp, BelgiumJeongmin HanDepartment of Biochemistry, College of Life Science & Biotechnology, Yonsei University, 134 Shinchon-Dong, Seodaemoon-Gu, Seoul, 120-749, KoreaSooho ChoiDepartment of Biochemistry, College of Life Science & Biotechnology, Yonsei University, 134 Shinchon-Dong, Seodaemoon-Gu, Seoul, 120-749, KoreaEun Ha ChoiDepartment of Electrical and Biological Physics, Kwangwoon University, Seoul, 01897, KoreaAnnemie BogaertsResearch Group PLASMANT, Department of Chemistry, University of Antwerp, Universiteitsplein 1, B-2610, Antwerp, Belgium. [email protected]Weontae LeeDepartment of Biochemistry, College of Life Science & Biotechnology, Yonsei University, 134 Shinchon-Dong, Seodaemoon-Gu, Seoul, 120-749, Korea. [email protected]
2018en
ABI

Аннотация

Cold atmospheric plasma (CAP) has great potential for sterilization in the food industry, by deactivation of thermophilic bacteria, but the underlying mechanisms are largely unknown. Therefore, we investigate here whether CAP is able to denature/modify protein from thermophilic bacteria. We focus on MTH1880 (MTH) from Methanobacterium thermoautotrophicum as model protein, which we treated with dielectric barrier discharge (DBD) plasma operating in air for 10, 15 and 20 mins. We analysed the structural changes of MTH using circular dichroism, fluorescence and NMR spectroscopy, as well as the thermal and chemical denaturation, upon CAP treatment. Additionally, we performed molecular dynamics (MD) simulations to determine the stability, flexibility and solvent accessible surface area (SASA) of both the native and oxidised protein.

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