Adsorção Física De Lipase Microbiana Em Matriz Hidrofóbica: Determinação De Parâmetros Bioquímicos E Termodinâmicos Dos Biocatalisadores Preparados

Abstract

RESUMO -Lipase deThermomyces lanuginosus (LTL) foi imobilizada em partículas de poli-hidroxibutirato (PHB) para a preparação de biocatalisadores ativos. Neste estudo, foram oferecidos carregamentos de proteína de 0,5 a 100 mg/g de suporte. A adsorção da enzima seguiu o modelo de Langmuir (R 2 =0,9704). Máxima atividade hidrolítica de 1300 UI/g de suporte e concentração de proteína imobilizada de 26,5 ± 1,80 mg/g foi alcançada.A imobilização da enzima realizada com carregamentos de proteína inferior a 3 mg exibiu hiperativação (atividade recuperada acima de 100%). A enzima livre mostrou máxima atividade hidrolítica em pH 8,0 e 60°C, enquanto que o biocatalisador preparado a pH 7,5 e 65°C. A imobilização aumentou ligeiramente a estabilidade térmica da enzima no intervalo de temperatura entre 30 e 50°C, confirmado por determinação dos parâmetros termodinâmicos energia livre de Gibbs (ΔG 0 ), entalpia (ΔH 0 ) e entropia (ΔS 0 ).

Improved synthesis of dietary triglycerides by using lipase supported on clay carriers

“…As the ROL is a 1,3‐specific enzyme, it is known that the largest DI that can be obtained is 66.67%, which demonstrates that the value obtained for the reactions with ROL@D‐Ac was satisfactory and adequate. [ 29 ] From the results obtained, the DIs of the reactions were calculated, resulting in 41.53% ± 3.99% for ROL@D‐Ac, 27.58% ± 1.68% for ROL@C‐Ac, and 34.53% for Lipozyme RM IM. Although this commercial lipase is widely used, [ 6,28 ] the DI obtained was lower than that using lipase from R. oryzae immobilized on diatomite (41.53% ± 3.99%), which confirms the potential of this support.…”

“…As the ROL is a 1,3-specific enzyme, it is known that the largest DI that can be obtained is 66.67%, which demonstrates that the value obtained for the reactions with ROL@D-Ac was satisfactory and adequate. [29] From the results obtained, the DIs of the reactions were calculated, resulting in 41.53% ± 3.99% for ROL@D-Ac, 27.58% ± 1.68% for ROL@C-Ac, and 34.53% for Lipozyme RM IM. Although this commercial lipase is widely used, [6,28] the DI obtained was lower than that using lipase from R. oryzae immobilized on The advantages for the use of studied clays, especially diatomite, are linked to the ease of supply of the material due to the diatomic deposits available in the world, simple obtaining by high fragmentation due to the heterogeneous composition of biosilica and other different diatomic species, low cost and porosity, favoring its use for immobilization of enzymes.…”