Unique Features of a New Baeyer–Villiger Monooxygenase from a Halophilic Archaeon

Autor: Francesco Filippini, Patrizia Polverino de Laureto, Mattia Niero, Irene Righetto, Elisa Beneventi, Marco W. Fraaije, Elisabetta Bergantino
Přispěvatelé: Biotechnology
Jazyk: angličtina
Rok vydání: 2020
Předmět:
ORGANIC-SOLVENTS
archaeon
bioconversions
ALPHA-AMYLASE
PROTEINS
In silico
Baeyer-Villiger monooxygenase
normal modes analysis
medicine.disease_cause
lcsh:Chemical technology
SEQUENCE
01 natural sciences
Catalysis
lcsh:Chemistry
03 medical and health sciences
Glucose dehydrogenase
medicine
Baeyer–Villiger monooxygenase
recombinant halophilic enzyme
protein electrostatics
CRYSTAL-STRUCTURE
lcsh:TP1-1185
GLUCOSE-DEHYDROGENASE
Physical and Theoretical Chemistry
Escherichia coli
030304 developmental biology
baeyer–villiger monooxygenase
chemistry.chemical_classification
0303 health sciences
PURIFICATION
010405 organic chemistry
CYCLOHEXANONE MONOOXYGENASE
SALT
Haloterrigena turkmenica
Monooxygenase
Halophile
0104 chemical sciences
Enzyme
chemistry
Halophilic archaeon
Biochemistry
lcsh:QD1-999
MALATE-DEHYDROGENASE
Zdroj: Catalysts, Vol 10, Iss 1, p 128 (2020)
Catalysts, 10(1):128. MDPI AG
Catalysts
Volume 10
Issue 1
ISSN: 2073-4344
Popis: Type I Baeyer&ndash
Villiger monooxygenases (BVMOs) are flavin-dependent monooxygenases that catalyze the oxidation of ketones to esters or lactones, a reaction otherwise performed in chemical processes by employing hazardous and toxic peracids. Even though various BVMOs are extensively studied for their promising role in industrial biotechnology, there is still a demand for enzymes that are able to retain activity at high saline concentrations. To this aim, and based on comparative in silicoanalyses, we cloned HtBVMO from the extremely halophilic archaeon Haloterrigena turkmenica DSM 5511. When expressed in standard mesophilic cell factories, proteins adapted to hypersaline environments often behave similarly to intrinsically disordered polypeptides. Nevertheless, we managed to express HtBVMO in Escherichia coli and could purify it as active enzyme. The enzyme was characterized in terms of its salt-dependent activity and resistance to some water&ndash
organic-solvent mixtures. Although HtBVMO does not seem suitable for industrial applications, it provides a peculiar example of an alkalophilic and halophilic BVMO characterized by an extremely negative charge. Insights into the behavior and structural properties of such salt-requiring may contribute to more efficient strategies for engineering the tuned stability and solubility of existing BVMOs.
Databáze: OpenAIRE
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