Improving the thermostability of xylanase a from bacillus subtilis by combining bioinformatics and electrostatic interactions optimization

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Autor(es): dc.contributorRice University-
Autor(es): dc.contributorUniversidade Estadual Paulista (Unesp)-
Autor(es): dc.contributorUniversity of Houston-
Autor(es): dc.creatorNgo, Khoa-
Autor(es): dc.creatorDa Silva, Fernando Bruno [UNESP]-
Autor(es): dc.creatorLeite, Vitor B. P.-
Autor(es): dc.creatorContessoto, Vinícius G.-
Autor(es): dc.creatorOnuchic, José N.-
Data de aceite: dc.date.accessioned2022-02-22T00:51:17Z-
Data de disponibilização: dc.date.available2022-02-22T00:51:17Z-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-06-25-
Data de envio: dc.date.issued2021-05-06-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1021/acs.jpcb.1c01253-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/207747-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/207747-
Descrição: dc.descriptionThe rational improvement of the enzyme catalytic activity is one of the most significant challenges in biotechnology. Most conventional strategies used to engineer enzymes involve selecting mutations to increase their thermostability. Determining good criteria for choosing these substitutions continues to be a challenge. In this work, we combine bioinformatics, electrostatic analysis, and molecular dynamics to predict beneficial mutations that may improve the thermostability of XynA from Bacillus subtilis. First, the Tanford-Kirkwood surface accessibility method is used to characterize each ionizable residue contribution to the protein native state stability. Residues identified to be destabilizing were mutated with the corresponding residues determined by the consensus or ancestral sequences at the same locations. Five mutants (K99T/N151D, K99T, S31R, N151D, and K154A) were investigated and compared with 12 control mutants derived from experimental approaches from the literature. Molecular dynamics results show that the mutants exhibited folding temperatures in the order K99T > K99T/N151D > S31R > N151D > WT > K154A. The combined approaches employed provide an effective strategy for low-cost enzyme optimization needed for large-scale biotechnological and medical applications.-
Descrição: dc.descriptionCenter for Theoretical Biological Physics Rice University-
Descrição: dc.descriptionDepartamento de Física Instituto de Biociências Letras e Ciencias Exatas Unesp-Univ. Estadual Paulista-
Descrição: dc.descriptionDepartment of Physics and Astronomy Center for Theoretical Biological Physics Rice University-
Descrição: dc.descriptionDepartment of Physics University of Houston-
Descrição: dc.descriptionDepartamento de Física Instituto de Biociências Letras e Ciencias Exatas Unesp-Univ. Estadual Paulista-
Formato: dc.format4359-4367-
Idioma: dc.languageen-
Relação: dc.relationJournal of Physical Chemistry B-
???dc.source???: dc.sourceScopus-
Título: dc.titleImproving the thermostability of xylanase a from bacillus subtilis by combining bioinformatics and electrostatic interactions optimization-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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