# Poly (Ethylene-Alt-Maleic Anhydride) Ionic Modification of Lipase B from Candida antarctica Immobilized on Octyl Agarose Beads Alters Its Catalytic Properties

## TL;DR

This study shows how modifying immobilized Candida antarctica lipase B with a polymer can significantly change its activity and stability, depending on various factors.

## Contribution

The study introduces a novel approach to altering lipase B properties through ionic modification with poly(ethylene-alt-maleic anhydride).

## Key findings

- Polymer modification can increase enzyme activity by more than double or reduce it by 5–6 times depending on conditions.
- Stability improvements were observed, such as maintaining 80% activity compared to 5% in unmodified biocatalysts under certain conditions.
- The modification prevents enzyme release during inactivation, indicating a structural stabilization effect.

## Abstract

The lipase B from Candida antarctica was immobilized on octyl-agarose using low and high (one that saturated the support surface with enzyme) loadings. Then, both biocatalysts were aminated, and the aminated and non-aminated biocatalysts were used in further experiments. The enzyme activity was determined using substrates with different structures. The modification of the four biocatalysts with poly (ethylene-alt-maleic anhydride) revealed that only a marginal covalent reaction occurs. That way, the ion exchange of the polymer on the immobilized enzyme surface should be responsible for the enzyme functional changes. The modification of the biocatalysts with this polymer produced mixed results for enzyme activity (depending on the enzyme loading, use of aminated or non-aminated enzyme, polymer concentration and used substrate), in some instances more than doubling the activity, in others reducing it by 5–6 times the activity when compared to the unmodified biocatalyst. The effects on biocatalyst stability were also mixed, depending on the same factors; in some instances, great stabilization could be found (e.g., in inactivation of the highly loaded aminated biocatalyst at pH 7.0, the unmodified biocatalyst kept 5% of the initial activity, while the biocatalyst modified with 1% of the polymer maintained 80%), but in other instances, enzyme stability was reduced after modification. It was shown that one of the effects of the polymer modification was the prevention of the enzyme release during inactivation.