Beauveria bassiana Lipase A expressed in Komagataella (Pichia) pastoris with potential for biodiesel catalysis

Autor(es):Mostrar menos -

Vici, Ana C. ^[1] ; da Cruz, Andrezza F. ^[2] ; Facchini, Fernanda D. A. ^[1] ; de Carvalho, Caio C. ^[2] ; Pereira, Marita G. ^[2] ; Fonseca-Maldonado, Raquel ^[3] ; Ward, Richard J. ^[3] ; Pessela, Benevides C. ^[4] ; Fernandez-Lorente, Gloria ^[4] ; Torres, Fernando A. G. ^[5] ; Jorge, Joao A. ^[2] ; Polizeli, Maria L. T. M. ^[2]

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, Dept Bioquim & Imunol, Fac Med Ribeirao Preto, BR-14040901 Ribeirao Preto, SP - Brazil

^[2] Univ Sao Paulo, Dept Biol, Fac Filosofia Ciencias & Letras Ribeirao Preto, BR-14040901 Ribeirao Preto, SP - Brazil

^[3] Univ Sao Paulo, Dept Quim, Fac Med Ribeirao Preto, BR-14040901 Ribeirao Preto, SP - Brazil

^[4] CSIC, Inst Invest Ciencias Alimentos, Dept Biotecnol & Microbiol Alimentos, Madrid - Spain

^[5] Univ Brasilia, Inst Ciencias Biol, Dept Biol Celular, Brasilia, DF - Brazil

• Tipo de documento: Artigo Científico
• Fonte: FRONTIERS IN MICROBIOLOGY; v. 6, OCT 7 2015.
• Citações Web of Science: 8

Resumo

Lipases (EC 3.1.1.3) comprise a biotechnologically important group of enzymes because they are able to catalyze both hydrolysis and synthesis reactions, depending on the amount of water in the system. One of the most interesting applications of lipase is in the biofuel industry for biodiesel production by oil and ethanol (or methanol) transesterification. Entomopathogenic fungi, which are potential source of lipases, are still poorly explored in biotechnological processes. The present work reports the heterologous expression and biochemical characterization of a novel Beauveria bassiana lipase with potential for biodiesel production. The His-tagged B. bassiana lipase A (BbLA) was produced in Komagataella pastoris in buffered methanol medium (BMM) induced with 1% methanol at 30 degrees C. Purified BbLA was activated with 0.05% Triton X-100 and presented optimum activity at pH 6.0 and 50 degrees C. N-glycosylation of the recombinant BbLA accounts for 31.5% of its molecular weight. Circular dichroism and molecular modeling confirmed a structure composed of a-helix and -sheet, similar to alpha/beta hydrolases. Immobilized BbLA was able to promote transesterification reactions in fish oil, demonstrating potential for biodiesel production. BbLA was successfully produced in K. pastoris and shows potential use for biodiesel production by the ethanolysis reaction. (AU)

• Processo FAPESP: 10/52322-3 - Bioprospecção de fungos filamentosos produtores de holoenzimas com aplicação em biorefinaria
• Beneficiário: Maria de Lourdes Teixeira de Moraes Polizeli
• Modalidade de apoio: Auxílio à Pesquisa - Programa BIOTA - Regular