Lipase production by Aspergillus brasiliensis in solid-state cultivation of malt bagasse in different bioreactors configurations

We evaluated the conditions to produce lipase in solid-state cultivation using a recently isolated strain of Aspergillus brasiliensis 157f in bioreactors of different confi gurations: static fl at-bed, plugged-fl ow bed with forced water-saturated aeration, and pilot-scale rotating drum bioreactor,...

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Detalles Bibliográficos
Autores: Eichler, Paulo, Bastiani, Daniela de, Santos, Fernando Almeida, Ayub, Marco Antônio Záchia
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2020
País:Brasil
Institución:Universidade Federal do Rio Grande do Sul (UFRGS)
Repositorio:Repositório Institucional da UFRGS
Idioma:inglés
OAI Identifier:oai:www.lume.ufrgs.br:10183/263906
Acceso en línea:http://hdl.handle.net/10183/263906
Access Level:acceso abierto
Palabra clave:Aspergillus
Lipase
Malte
Transesterificação
Aspergillus brasiliensis
Brewery’s spent malt
Lipase production
Solid-state cultivation
Transesterification reaction
Descripción
Sumario:We evaluated the conditions to produce lipase in solid-state cultivation using a recently isolated strain of Aspergillus brasiliensis 157f in bioreactors of different confi gurations: static fl at-bed, plugged-fl ow bed with forced water-saturated aeration, and pilot-scale rotating drum bioreactor, using malt bagasse as substrate. Lipase production was optimized applying experimental design analysis, which showed optima parameters defi ned as pH 7.7, addition of 11.3 % of soybean oil to the medium, and culture temperature of 32.7 o C, in static fl at-bed. The highest enzyme activity (9.8 U.g-1 substrate) was obtained in the plugged-fl ow bed with forced water-saturated aeration. The fermented culture medium was lyophilized to create a solid enzymatic preparation (SEP), which was used to test the possibility of using this cheap biocatalyst in bioreactors to mediate esterifi cation and transesterifi cation reactions. SEP presented lipase activities of 7.35 U.g-1 substrate, indicating the possibility of further enhancing aspects of the use of such biocatalyst.