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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Low-resolution envelope, biophysical analysis and biochemical characterization of a short-chain specific and halotolerant carboxylesterase from Bacillus licheniformis

Texto completo
Autor(es):
Nakamura, Aline M. [1] ; Seiki Kadowaki, Marco Antonio [1] ; Godoy, Andre [1] ; Nascimento, Alessandro S. [1] ; Polikarpov, Igor [1]
Número total de Autores: 5
Afiliação do(s) autor(es):
[1] Univ Sao Paulo, Sao Carlos Inst Phys, Av Trabalhador Sao Carlense 400, BR-13566590 Sao Carlos, SP - Brazil
Número total de Afiliações: 1
Tipo de documento: Artigo Científico
Fonte: International Journal of Biological Macromolecules; v. 120, n. B, p. 1893-1905, DEC 2018.
Citações Web of Science: 0
Resumo

Esterases are widely applied in industrial processes due to their versatility, regio- and enantioselectivity, lack of cofactors and stability in organic solvents. Bacillus licheniformis, a microorganism frequently used in industrial and biotechnological applications such as dairy, baking, beverage, pulp and paper, detergent and cosmetics production, organic synthesis and waste management, is a promising source of esterases. Here we describe the biochemical and biophysical characterization of B. licheniformis carboxylesterase BlEst1 and its SAXS-derived molecular envelope. BlEst1 has optimal hydrolytic activity against p-nitrophenyl acetate at pH 7.0 and 40 degrees C. Furthermore, BlEst1 is stable in different organic solvents such as methanol, isopropanol and butanol. The BlEst1 homology model reveals a typical alpha/beta hydrolase core with an adjacent auxiliary domain, snuggly fitting the experimental low-resolution SAXS molecular envelope. Moreover, BlEst1 maintained considerable part of its activity in the presence of up to 5 M NaCl and its thermal stability was significantly enhanced by the presence of salt, revealing its halotolerant character. The ability to work under harsh conditions makes BlEst1 an interesting candidate for industrial applications. (C) 2018 Elsevier B.V. All rights reserved. (AU)

Processo FAPESP: 11/20505-4 - Duas classes importantes de glicosil hidrolases: estudos funcionais e análise estrutural
Beneficiário:Marco Antonio Seiki Kadowaki
Linha de fomento: Bolsas no Brasil - Pós-Doutorado