In vitro and in silico characterization of a novel dextranase from Pochonia chlamydosporia
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The objective of this study was to purify, characterize, and phylogenetically and structurally analyze the dextranase produced by the fungus Pochonia chlamydosporia. Dextranase produced by the fungus P. chlamydosporia was purified to homogeneity in two steps, with a yield of 152%, purification factor of 6.84 and specific activity of 358.63 U/mg. Its molecular weight was estimated by SDS-PAGE at 64 kDa. The enzyme presented higher activity at 50 °C and pH 5.0, using 100 mM citrate–phosphate buffer, was inhibited by Ag1+, Hg2+, Cu2+, Mg2+, and presented KM of 23.60 µM. Mature dextranase is composed of 585 amino acids residues, with a predicted molecular weight of 64.38 kDa and pI 5.96. This dextranase showed a strong phylogenetic similarity when compared to Trichoderma harzianum dextranase. Its structure consists of two domains: the first composed by 15 β strands, and the second composed by a right-handed parallel β-helix.
KeywordsEnzyme Verticillium chlamydosporium Purification 3D structure
The authors would like to thank the Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES), the Fundação de Amparo à Pesquisa de Minas Gerais (FAPEMIG), and the Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) for the financial support.
Compliance with ethical standards
Conflicts of interest
The authors declare that they have no conflict of interest.
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