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Updated: Jun 5, 2026
Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Concentration, partial characterization, and immobilization of lipase extract from P. brevicompactum by solid-state
Marceli Fernandes Silva1, Denise M G Freire, Aline Machado de Castro
1Departamento de Engenharia de Alimentos, URI-Campus de Erechim, Av. Sete de Setembro 1621, Erechim, 99700-000, Brazil.
Abstract:
One relevant limitation hindering the industrial application of microbial lipases has been attributed to their production cost, which is determined by the production yield, enzyme stability among other. The objective of this work was to evaluate the concentration and immobilization of lipase extracts from Penicillium brevicompactum obtained by solid-state fermentation of babassu cake and castor bean cake. The precipitation with ammonium sulfate 60% of saturation of crude extract obtained with babassu cake as raw material showed an enhancement in hydrolytic and esterification activities from 31.82 to 227.57 U/g and from 170.92 to 207.40 U/g, respectively. Concentrated lipase extracts showed preference to medium-chain triglycerides and fatty acids. It is shown that the enzyme activity is maintained during storage at low temperatures (4 and -10°C) for up to 30 days. Higher esterification activities were achieved when the lipase extract was immobilized in sodium alginate and activated coal.
