Influence of the morphology of core-shell supports on the immobilization of lipase B from Candida antarctica.

Martina Pinto,José Pinto,Denise Freire

doi:10.3390/molecules190812509

Martina Pinto, José Pinto + Show 1 more

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https://doi.org/10.3390/molecules190812509

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Abstract

Core-shell polymer particles with different properties were produced through combined suspension-emulsion polymerizations and employed as supports for immobilization of lipase B from Candida antarctica. In order to evaluate how the morphology of the particles affects the immobilization parameters, empirical models were developed to describe the performance of the biocatalysts as a function of the specific area, volume of pores and average pore diameter of the supports. It was observed that the average pore sizes did not affect the enzymatic activities in the analyzed range of pore sizes. It was also observed that the increase of the specific area (and of the volume of pores) led to higher enzyme loadings, also leading to an increase in the esterification activity, as expected. However, when the specific area (and volume of pores) increased, the hydrolytic activity and the retention of hydrolytic activity of the biocatalysts decreased, indicating the existence of diffusional limitations for some hydrolytic reactions, probably because of the high reaction rates.

Highlights

Among enzymes, lipases have received considerable attention both in the scientific literature and in the commercial market [1]
It is important to observe that, the core particles exhibited very low specific areas, significant amounts of enzyme were absorbed by core particles, probably because of the interaction forces that exist between the lipases and the hydrophobic surfaces of the supports [5]
This supports the idea that the observed decrease of hydrolytic activity was caused by the increase of the amount of protein adsorbed onto the supports surfaces during the immobilization process

Summary

Introduction

Lipases have received considerable attention both in the scientific literature and in the commercial market [1]. Lipases can catalyze different reactions, including hydrolysis, esterification and transesterification reactions, with high selectivity and specificity [2,3,4,5]. For this reason, lipases find widespread use in many different areas, including applications in the food, pharmaceutical, cosmetics and biosensors fields [1,6]. Soluble enzymes cannot be recovered at the end of the reaction process, which limits the development of continuous operations and increases the operation costs, as enzymes with the desired degree of purity are usually very expensive. Improvement of enzyme performance can be related to modification of the enzyme structure (due to chemical and physical interaction with the support), generation of a more favorable reaction environment in the surroundings of the enzymes (due to interaction of the support with the reactants and solvents), existence of diffusional limitations (modifying concentration gradients along the pores), among others [16,17,18,19,20,21]

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