Navegando por Autor "Scherer, Robison P."
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Artigo Immobilization of porcine pancreatic lipase in zeolite MCM 22 with different Si/Al ratios(Elsevier, 2011-02-28) Calgaroto, Cléber; Scherer, Robison P.; Calgaroto, Selma; Oliveira, Jose Vladimir; Oliveira, Débora de; Pergher, Sibele Berenice CastellãThe use of zeolites as support for immobilization of enzymes has been a matter of great interest recently due to the potential properties of these materials. In this work, the MCM 22 zeolite with different Si/Al ratios (15, 25 and 50) was used as support for immobilization of porcine pancreatic lipase, assessing the effect of its structure on the immobilization yield and enzyme activity. Results showed that the material composition influenced significantly the immobilization process. Higher yields of immobilization and enzymatic activities were achieved when MCM 22 with Si/Al ratio of 25 was used as support. In general, results demonstrate the potential of MCM 22 as support for porcine pancreatic lipase immobilization.Artigo Influence of process parameters on the immobilization of commercial porcine pancreatic lipase using three low-cost supports(Elsevier, 2012-10) Scherer, Robison P.; Dallago, Rogério L.; Penna, Fábio G.; Bertella, Francile; Oliveira, Débora de; Oliveira, Jose Vladimir de; Pergher, Sibele Berenice CastellãThe use of lipases as biocatalysts has attracted much attention recently, but industrial application has been hindered mainly due to the high production cost, determined by the production yield and enzyme stability. Immobilization of biocatalysts in inert supports can ensure their use for several batches, making possible to build cost-effective processes. The objective of this work was to investigate the influence of immobilization time and enzyme to support mass ratio on the yield of immobilization and esterification activity of porcine pancreatic lipase. Higher immobilization yields (38.2%) were obtained for pillared montmorillonite, 120 min of immobilization and enzyme to support mass ratio of 2:0.5. The highest esterification activity (1403 U/g) was achieved using the montmorillonite, after 180 min of immobilization and enzyme to support ratio of 2:1. The characterization of the supports, free and immobilized enzyme on different supports made possible to elucidate the immobilization results through the knowledge of support features.Artigo Natural montmorillonite as support for the immobilization of inulinase from Kluyveromyces marxianus NRRL Y-7571(Elsevier, 2012-10) Coghetto, Chaline C.; Scherer, Robison P.; Silva, Marceli F.; Golunski, Simone; Pergher, Sibele Berenice Castellã; Oliveira, Débora de; Oliveira, J. Vladimir; Treichel, HelenThe objective of this study was to investigate the process of immobilization of inulinases using natural montmorillonite as inorganic support. The enzyme to buffer ratio of 3:10 and 10 min of immobilization led to the highest specific activity, 375.07 U/mg protein. The immobilized inulinase kept its activity after 1968 h under storage at low temperatures and after 456–1826 h at high temperatures. The pH value of 3.5 led to the highest specific activity. Km values of 1.46 and 0.38 mM, and vmax of 0.2487 and 0.2396 mol/L min, were obtained, respectively, for sucrose and inulin.