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      Aproveitamento de resíduos da agroindústria do óleo de dendê para a produção de lipase por Aspergillus Níger Translated title: Agro-industrial residues utilization of palm oil for lipase production by Aspergillus niger

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          Abstract

          RESUMO: Neste trabalho, foi avaliado o desempenho de duas linhagens de Aspergillus niger (mutante 11T53A14 e selvagem C) previamente selecionadas como promissoras para a produção de lipases, utilizando meios de cultivo formulados a partir da torta de dendê (palmiste) e da borra alcalina do refino do óleo de dendê (borra de dendê), resíduos provenientes da agroindústria do óleo de dendê (palma) por fermentação em estado sólido (FES). Os experimentos de produção da enzima em FES foram conduzidos em colunas aeradas, incubadas em banho-maria a 32ºC com entrada controlada de ar não umedecido de 1,0vvm. Os melhores resultados foram obtidos com a cepa mutante A. niger 11T53A14 em meio contendo torta de dendê umedecida com solução sulfato de amônio (1,2%) e com a adição de 3% da borra de dendê. O valor máximo da atividade da lipase neste meio foi de 72,57U gss-1 em 48 horas. Esse valor foi 47,5% superior ao obtido no meio sem a borra de dendê. A comparação do desempenho da cepa mutante com a cepa selvagem mostrou que o meio composto por torta de dendê adicionado com sulfato de amônio e borra de dendê induziu ambas as linhagens a produzir lipases com bons níveis de atividade, além de reduzir o tempo de processo de fermentação.

          Translated abstract

          ABSTRACT: In this paper it was evaluated the performance of two strains of Aspergillus niger (mutant 11T53A14 and wild type C) previously selected as promising for lipase production, from cultivation media formulated from palm kernel cake (kernel) and alkaline sludge from refining were evaluated palm oil (palm oil sludge), palm oil (palm) waste industrialization by solid state fermentation (SSF). Experiments of enzyme production in SSF were conducted in aerated columns, incubated in a water bath at 32°C with controlled inlet of 1.0vvm. The best results were obtained with the mutant strain A. niger 11T53A14 in medium containing palm kernel cake moistened with a solution of ammonium sulfate (1.2%) and with the addition of 3% of palm oil sludge. The maximum lipase activity in this medium was 72.57U gdw-1 in 48 hours and 47.5% higher than in the medium without sludge palm. A comparison of the performance of the mutant strain with the wild-type strain showed that the medium composed of palm kernel cake added with ammonium sulfate and blurs palm induced both strains to produce lipases with good activity levels and reduced the time of the fermentation process.

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          Protein measurement with the Folin phenol reagent.

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            Modificação de óleos e gorduras por biotransformação

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              Topological characterization and modeling of the 3D structure of lipase from Pseudomonas aeruginosa.

              Lipase from Pseudomonas aeruginosa is a M(r) 29 kDa protein with a single functional disulfide bond as shown by a shift in electrophoretic mobility after treatment with dithiothreitol and iodoacetamide. Limited proteolysis of lipase with Staphylococcus aureus protease V8 resulted in cleavage after amino acid residues Asp38 and Glu46. Comparison of the lipase amino acid sequence with those of other hydrolases with known 3D structures indicated that the folding pattern might be compatible with the alpha/beta hydrolase fold, thereby allowing us to construct a 3D model which fitted the biochemical properties. The model predicts a catalytic triad consisting of Ser82, Asp229 and His251, and contains a disulfide bond connecting residues Cys183 and Cys235. Residues Asp38 and Glu46 are located at the surface of the enzyme, whereas the disulfide bond is rather inaccessible, which is in agreement with the finding that the protein needed to be partly unfolded before a reduction of the disulfide bond could take place. A striking prediction from the model was the lack of a lid-like alpha-helical loop structure covering the active site which confers to other well-characterized lipases a unique property known as interfacial activation. Experimental determination of lipase activity under conditions where the substrate existed either as monomeric solutions or aggregates confirmed the absence of interfacial activation.
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                Author and article information

                Contributors
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Journal
                cr
                Ciência Rural
                Cienc. Rural
                Universidade Federal de Santa Maria
                1678-4596
                April 2016
                : 46
                : 4
                : 755-761
                Affiliations
                [1 ] Embrapa Agroindústria de Alimentos Brazil
                [2 ] Centro Universitário Estadual da Zona Oeste Brasil
                [3 ] Embrapa Agroenergia Brazil
                Article
                S0103-84782016000400755
                10.1590/0103-8478cr20131673
                741ca2c4-eca1-4b75-8640-bcb3b61f06b1

                This work is licensed under a Creative Commons Attribution 4.0 International License.

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                SciELO Brazil

                Self URI (journal page): http://www.scielo.br/scielo.php?script=sci_serial&pid=0103-8478&lng=en
                Categories
                AGRONOMY

                Horticulture
                lipase,resíduo agroindustrial,Aspergillus niger,agro-industrial residue
                Horticulture
                lipase, resíduo agroindustrial, Aspergillus niger, agro-industrial residue

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