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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 molecular shape, biochemical characterization and emulsification properties of a halotolerant esterase fromBacillus licheniformis

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Author(s):
Leite, Ana Elisa T. [1] ; Briganti, Lorenzo [1] ; de Araujo, Evandro Ares [1] ; Arnoldi Pellegrini, Vanessa de Oliveira [1] ; Camilo, Cesar Moyses [1] ; Polikarpov, Igor [1]
Total Authors: 6
Affiliation:
[1] Univ Sao Paulo, Sao Carlos Inst Phys, Sao Carlos, SP - Brazil
Total Affiliations: 1
Document type: Journal article
Source: EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS; v. 49, n. 6 JUL 2020.
Web of Science Citations: 0
Abstract

Bacterial esterases are highly versatile enzymes, currently widely used in detergents, biosurfactants, bioemulsifiers and as biocatalysts in paper and food industries. Present work describes heterologous expression, purification, and biophysical and biochemical characterization of a halotolerant esterase fromBacillus licheniformis(BlEstA).BlEstA preferentially cleavespNP-octanoate and both activity and stability of the enzyme increased in the presence of 2 M NaCl, and also with several organic solvents (ethanol, methanol and DMSO). Furthermore,BlEstA has considerable emulsifying properties, particularly with olive oil as substrate. Our studies also show that the enzyme is monomeric in solution and its small-angle X-ray scattering low-resolution molecular envelope fits well its high-resolution homology model. (AU)

FAPESP's process: 15/13684-0 - Structural and functional studies of enzymes that participate in complex carbohydrates synthesis and degradation
Grantee:Igor Polikarpov
Support Opportunities: Research Projects - Thematic Grants