Biotechnology and Bioprocess Engineering 2024; 29(6): 1149-1163  
Immobilization study of a monomeric oleate hydratase from Rhodococcus erythropolis
Maria Bandookwala 1 · Sophia A. Prem 1 · Kathrin L. Kollmannsberger 2 · Michael Zavrel 3 · Daniel Garbe 1 · Thomas Brück 1
1 Werner Siemens-Chair of Synthetic Biotechnology, TUM School of Natural Sciences, Technical University of Munich, 85748 Garching, Germany
2 Department of Chemistry, TUM School of Natural Sciences, Technical University of Munich, 85748 Garching, Germany
3 Bioprocess Engineering, TUM Campus Straubing for Biotechnology and Sustainability, Technical University of Munich, 94315 Straubing, Germany
Correspondence to: ✉ Thomas Brück
brueck@tum.de
Received: January 16, 2024; Revised: June 19, 2024; Accepted: June 26, 2024; Published online: July 2, 2024.
© The Korean Society for Biotechnology and Bioengineering. All rights reserved.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract
The chemical, pharmaceutical, and cosmetic industries are currently confronted with the challenge of transitioning from traditional chemical processes to more sustainable biocatalytic methods. To support that aim, we developed various heterogeneous biocatalysts for an industrially relevant enzyme called oleate hydratase that converts oleic acid to 10-hydroxystearic acid, a fatty emollient substance useful for various technical applications. We used cheap support matrices such as silica, chitosan, cellulose, and agarose for further scale-up and economic feasibility at the industrial level alongside more sophisticated supports like metal–organic frameworks. Different physical and chemical binding approaches were employed. Particularly, by immobilizing oleate hydrates on a 3-aminopropyltriethoxysilane surface-functionalized cellulose matrix, we developed an enzyme immobilizate with almost 80% activity of the free enzyme. The long-term goal of this work was to be able to use the developed heterogeneous biocatalyst for multiple reuse cycles enabling profi table biocatalysis. Despite high initial conversion rate by the developed cellulose-based immobilizate, a depletion in enzyme activity of immobilized oleate hydratase was observed over time. Therefore, further enzyme modification is required to impart stability, the optimization of operational conditions, and the development of carrier materials that enable economical and sustainable enzymatic conversion of oleic acid to meet the commercial demand.
Keywords: Oleate hydratase · Immobilization · 10-hydroxystearic acid · Chitosan · Cellulose · Rhodococcus erythropolis

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