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

Autor(es)

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]

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, Sao Carlos Inst Phys, Sao Carlos, SP - Brazil

• Tipo de documento: Artigo Científico
• Fonte: EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS; v. 49, n. 6 JUL 2020.
• Citações Web of Science: 0

Resumo

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)

• Processo FAPESP: 15/13684-0 - Estudos estruturais e funcionais de enzimas que participam na síntese e degradação de carboidratos complexos
• Beneficiário: Igor Polikarpov
• Modalidade de apoio: Auxílio à Pesquisa - Temático