MBSP1: a biosurfactant protein derived from a metagenomic library with activity in oil degradation

• Autor(a) principal: Araújo, Sinara Carla da Silva
• Data de Publicação: 2020
• Outros Autores: Portela, Rita de Cássia Barreto da Silva, Lima, Daniel Chaves de, Fonseca, Marbella Maria Bernardes, Araujo, Wydemberg Jose de, Silva, Uaska Bezerra e, Napp, Amanda Pasinato, Pereira, José Evandro Saraiva, Vainstein, Marilene Henning, Lima, Lucymara Fassarella Agnez
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UFRGS
• Texto Completo: http://hdl.handle.net/10183/267555
• topic: Escherichia coli; Genética de microorganismos

Microorganisms represent the most abundant biomass on the planet; however, because of several cultivation technique limitations, most of this genetic patrimony has been inaccessible. Due to the advent of metagenomic methodologies, such limitations have been overcome. Prevailing over these limitations enabled the genetic pool of non-cultivable microorganisms to be exploited for improvements in the development of biotechnological products. By utilising a metagenomic approach, we identifed a new gene related to biosurfactant production and hydrocarbon degradation. Environmental DNA was extracted from soil samples collected on the banks of the Jundiaí River (Natal, Brazil), and a metagenomic library was constructed. Functional screening identifed the clone 3C6, which was positive for the biosurfactant protein and revealed an open reading frame (ORF) with high similarity to sequences encoding a hypothetical protein from species of the family Halobacteriaceae. This protein was purifed and exhibited biosurfactant activity. Due to these properties, this protein was named metagenomic biosurfactant protein 1 (MBSP1). In addition, E. coli RosettaTM (DE3) strain cells transformed with the MBSP1 clone showed an increase in aliphatic hydrocarbon degradation. In this study, we described a single gene encoding a protein with marked tensoactive properties that can be produced in a host cell, such as Escherichia coli, without substrate dependence. Furthermore, MBSP1 has been demonstrated as the frst protein with these characteristics described in the Archaea or Bacteria domains.