Characterization of esterase activity from an Acetomicrobium hydrogeniformans enzyme with high structural stability in extreme conditions

Autor(es):Mostrar menos -

Kumagai, patricia S. ^[1] ; Gutierrez, Raissa F. ^[1] ; Lopes, Jose L. S. ^[2] ; Martins, Julia M. ^[1] ; Jameson, David ^[3] ; Castro, Aline M. ^[4] ; Martins, Luiz F. ^[4] ; DeMarco, Ricardo ^[1] ; Bossolan, Nelma R. S. ^[1] ; Wallace, B. A. ^[5] ; Araujo, Ana P. U. ^[1]

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, Dept Fis & Ciencia Interdisciplinar, Inst Fis Sao Carlos, Av Joao Dagnone 1100, BR-13563120 Sao Carlos, SP - Brazil

^[2] Univ Sao Paulo, Dept Fis Aplicada, Inst Fis, Rua Matao 1371, BR-05508090 Sao Paulo, SP - Brazil

^[3] Univ Hawaii Manoa, Dept Cell & Mol Biol, 1960 East West Rd, Honolulu, HI 96822 - USA

^[4] Petrobras SA, Ctr Pesquisas & Desenvolvimento CENPES, Gerencia Biotecnol, Av Horacio Macedo 950, BR-21941915 Rio De Janeiro, RJ - Brazil

^[5] Univ London, Birkbeck Coll, Inst Struct & Mol Biol, Malet St, London WC1E 7HX - England

• Tipo de documento: Artigo Científico
• Fonte: EXTREMOPHILES; v. 22, n. 5, p. 781-793, SEP 2018.
• Citações Web of Science: 3

Resumo

The biotechnological and industrial uses of thermostable and organic solvent-tolerant enzymes are extensive and the investigation of such enzymes from microbiota present in oil reservoirs is a promising approach. Searching sequence databases for esterases from such microbiota, we have identified in silico a potentially secreted esterase from Acetomicrobium hydrogeniformans, named AhEst. The recombinant enzyme was produced in E. coli to be used in biochemical and biophysical characterization studies. AhEst presented hydrolytic activity on short-acyl-chain p-nitrophenyl ester substrates. AhEst activity was high and stable in temperatures up to 75 A degrees C. Interestingly, high salt concentration induced a significant increase of catalytic activity. AhEst still retained 5 similar to 0% of its activity in 30% concentration of several organic solvents. Synchrotron radiation circular dichroism and fluorescence spectroscopies confirmed that AhEst displays high structural stability in extreme conditions of temperature, salinity, and organic solvents. The enzyme is a good emulsifier agent and is able to partially reverse the wettability of an oil-wet carbonate substrate, making it of potential interest for use in enhanced oil recovery. All the traits observed in AhEst make it an interesting candidate for many industrial applications, such as those in which a significant hydrolytic activity at high temperatures is required. (AU)

• Processo FAPESP: 15/50347-2 - Estudos biofísicos da estrutura/função de peptídeos antimicrobianos e enzimas isoladas de organismos extremófilos
• Beneficiário: Ana Paula Ulian de Araujo
• Modalidade de apoio: Auxílio à Pesquisa - Regular