Immobilization of Amano AK Lipase from Pseudomonas fluorescens on Novel Silk Microfiber using Oxone®: Parameter Optimization for Enzymatic Assays and use in Esterification of Residual Palm Oil

Author:

Júnior Evaldo B.M.1,Neves Fernando B.1,Lopes Samuel Q.1,Holanda Fabrício H.1,Souza Tiago M.2,Pinto Erveton P.3,Oliveira Alex N.1,Fonseca Luis P.4,Yoshioka Sérgio A.5,Ferreira Irlon M.1ORCID

Affiliation:

1. Laboratório de Biocatalise e Sintese Organica Aplicada, Universidade Federal do Amapa, Rod. Juscelino Kubitschek, Km 02, Jardim Marco Zero, 68902-280, Macapa, AP, Brazil

2. Departamento de Engenharia Quimica, Universidade do Estado do Amapa, 68900-070 Macapa, AP, Brazil

3. Departamento de Ciencias Exatas e Tecnologicas, Universidade Federal do Amapa, Rod. Juscelino Kubitschek, Km 02, Jardim Marco Zero, 68902-280, Macapa, AP, Brazil

4. Bioengineering Department, Instituto Superior Tecnico, University of Lisbon, Institute for Bioengineering and Biosciences, Av. Rovisco Pais, 1049-001 Lisbon, Portugal

5. Instituto de Quimica de Sao Carlos, Universidade de Sao Paulo, Av. Trabalhador Sao-Carlense, 400, J. Arnold Schimidt, 13563-590, Sao Carlos, SP, Brazil

Abstract

Background: Biodiesel has been shown to be effectively produced by immobilized enzymatic catalysts. The selection of support material is a prominent factor for obtaining an efficient lipase. Silk fibroin (SF) is a natural polymer produced by glands of some arthropods, especially by the Bombyx mor, attracting attention for immobilization of lipase. Objective: This paper presents a novel method to obtain silk microfibers (SMF) from Oxone® salt in water, used as support for Amano AK lipase from Pseudomonas fluorescens in biodiesel production from deodorization distillate of palm oil (DDPO). Method: The oxone® salt in the presence of Ca2+ ions acts as a mineralizing agent in the peptide bonds present in silk fibroin, altering some of its physical and chemical properties, such as zeta potential, crystallinity, micro-morphology, infrared spectroscopic profile, and showing formation or absence of SF original connections. Results: The modified support was tested as a support alternative for the immobilization of Amano AK lipase from Pseudomonas fluorescens. Enzyme activity values indicated that lipase immobilization on SMF was efficient as a heterogeneous catalyst in the esterification of DDPO (deodorization distillate palm oil). Conclusion: The effect of some reaction parameters, such as catalyst concentration, molar ratio, temperature, and reaction time, was studied to optimize the conditions for maximum conversion of DDPO (40.5%).

Funder

FAPEAP/CAPES

Publisher

Bentham Science Publishers Ltd.

Subject

General Medicine

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