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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.)

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

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Author(s):
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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]
Total Authors: 12
Affiliation:
[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
Total Affiliations: 5
Document type: Journal article
Source: FRONTIERS IN MICROBIOLOGY; v. 6, OCT 7 2015.
Web of Science Citations: 8
Abstract

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)