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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Nakamura, Aline M. [1] ; Seiki Kadowaki, Marco Antonio [1] ; Godoy, Andre [1] ; Nascimento, Alessandro S. [1] ; Polikarpov, Igor [1]
Total Authors: 5
Affiliation:
[1] Univ Sao Paulo, Sao Carlos Inst Phys, Av Trabalhador Sao Carlense 400, BR-13566590 Sao Carlos, SP - Brazil
Total Affiliations: 1
Document type: Journal article
Source: International Journal of Biological Macromolecules; v. 120, n. B, p. 1893-1905, DEC 2018.
Web of Science Citations: 0
Abstract

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)

FAPESP's process: 11/20505-4 - Two important classes of glycosyl hydrolases: functional studies and structural analysis
Grantee:Marco Antonio Seiki Kadowaki
Support type: Scholarships in Brazil - Post-Doctorate