Immobilization of Oleate Hydratase on Solid Supports

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Main Authors: Keiko Oike, Rob Schoevaart, Frank Hollmann, Ulf Hanefeld, Peter‐Leon Hagedoorn
Format: Artículo Open Access
Published: Wiley 2024
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author Keiko Oike
Rob Schoevaart
Frank Hollmann
Ulf Hanefeld
Peter‐Leon Hagedoorn
author_facet Keiko Oike
Rob Schoevaart
Frank Hollmann
Ulf Hanefeld
Peter‐Leon Hagedoorn
Keiko Oike
Rob Schoevaart
Frank Hollmann
Ulf Hanefeld
Peter‐Leon Hagedoorn
collection Wiley Open Access
contents Immobilization of Oleate Hydratase on Solid Supports Keiko Oike Rob Schoevaart Frank Hollmann Ulf Hanefeld Peter‐Leon Hagedoorn ChemCatChem AbstractOleate hydratases open a biocatalytic access to hydroxy fatty acids by hydration of unsaturated fatty acids. Their practical applicability, however, is hampered by their low stability. In this study we report the immobilization of the oleate hydratase from Rhodococcus erythropolis PR4 on functionalized porous, spherical polymer beads. Different carrier materials promoting covalent, hydrophobic, ionic and his‐tag affinity were screened and immobilization yields typically >95 % were observed. The highest activity recovery of 32 % was achieved by immobilization via ionic interaction with quaternary ammonium functionalized beads. Biochemical properties of the enzyme immobilized via ionic interaction remain unchanged upon immobilization. The immobilized enzyme was applied for synthesis of 10‐hydroxystearic acid remaining stable under process conditions. Conversion of up to 100 mM oleic acid gave 10‐hydroxystearic acid achieving a TON of up to 19,000. Successful recycling of the biocatalyst for up to ten cycles further demonstrate its potential for the synthesis of 10‐hydroxystearic acid. 10.1002/cctc.202301708 http://creativecommons.org/licenses/by/4.0/
doi_str_mv 10.1002/cctc.202301708
format Artículo Open Access
id wiley_oa_10_1002_cctc_202301708
institution Wiley Open Access
license_str_mv http://creativecommons.org/licenses/by/4.0/
publishDate 2024
publisher Wiley
record_format wiley_oa
spellingShingle Immobilization of Oleate Hydratase on Solid Supports
Keiko Oike
Rob Schoevaart
Frank Hollmann
Ulf Hanefeld
Peter‐Leon Hagedoorn
ChemCatChem
Immobilization of Oleate Hydratase on Solid Supports Keiko Oike Rob Schoevaart Frank Hollmann Ulf Hanefeld Peter‐Leon Hagedoorn ChemCatChem AbstractOleate hydratases open a biocatalytic access to hydroxy fatty acids by hydration of unsaturated fatty acids. Their practical applicability, however, is hampered by their low stability. In this study we report the immobilization of the oleate hydratase from Rhodococcus erythropolis PR4 on functionalized porous, spherical polymer beads. Different carrier materials promoting covalent, hydrophobic, ionic and his‐tag affinity were screened and immobilization yields typically >95 % were observed. The highest activity recovery of 32 % was achieved by immobilization via ionic interaction with quaternary ammonium functionalized beads. Biochemical properties of the enzyme immobilized via ionic interaction remain unchanged upon immobilization. The immobilized enzyme was applied for synthesis of 10‐hydroxystearic acid remaining stable under process conditions. Conversion of up to 100 mM oleic acid gave 10‐hydroxystearic acid achieving a TON of up to 19,000. Successful recycling of the biocatalyst for up to ten cycles further demonstrate its potential for the synthesis of 10‐hydroxystearic acid. 10.1002/cctc.202301708 http://creativecommons.org/licenses/by/4.0/
title Immobilization of Oleate Hydratase on Solid Supports
topic ChemCatChem
url https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cctc.202301708