Eco‐Friendly and Economical Approach for Immobilization of Thermostable ω‐Transaminase

The advent of recombinant enzymes as catalysts for biochemical transformation is a promising approach to efficiently obtain fine chemicals compared to traditional synthesis. However, the high cost, low stability, and limited reusability make soluble enzymes unsuitable for large‐scale applications. To obtain a thermally and operationally stable biocatalyst, enzymes isolated from extremophiles are isolated and bound on an appropriate support material, which helps preserve the structure of the enzyme and extend its usage. Herein, we report the immobilization of thermostable ω‐Transaminase (ω‐Ta) enzyme on diatomaceous earth as a readily available, easy‐to‐modify surface and a cost‐effective silica support. The supramolecular metal‐organic complexes of Fe 3+ and tannic acid were used as an eco‐friendly immobilization technique for ω‐Ta binding. The immobilized enzyme maintained the optimal pH, temperature, and storage stability as the soluble enzyme. The immobilized enzyme showed good reusability, retaining over 50% of its initial activity after five cycles. The utility of the modified support was also demonstrated for one‐step purification and immobilization of the enzyme. These results demonstrate a straightforward, economical, and environmentally benign approach to enzyme immobilization for industrial application.

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Publication Details

Journal
Chemistry - Methods
Published
2026-05-01
DOI
https://doi.org/10.1002/cmtd.70117
Primary Topic
Enzyme Catalysis and Immobilization
Type
article
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article

Eco‐Friendly and Economical Approach for Immobilization of Thermostable ω‐Transaminase

Divya Gaur, Wasia Khanam, Nidhi C. Dubey, Bijay P. Tripathi
Chemistry - Methods
Enzyme Catalysis and Immobilization
article

Eco‐Friendly and Economical Approach for Immobilization of Thermostable ω‐Transaminase

Divya Gaur, Wasia Khanam, Nidhi C. Dubey, Bijay P. Tripathi
article en

Abstract

The advent of recombinant enzymes as catalysts for biochemical transformation is a promising approach to efficiently obtain fine chemicals compared to traditional synthesis. However, the high cost, low stability, and limited reusability make soluble enzymes unsuitable for large‐scale applications. To obtain a thermally and operationally stable biocatalyst, enzymes isolated from extremophiles are isolated and bound on an appropriate support material, which helps preserve the structure of the enzyme and extend its usage. Herein, we report the immobilization of thermostable ω‐Transaminase (ω‐Ta) enzyme on diatomaceous earth as a readily available, easy‐to‐modify surface and a cost‐effective silica support. The supramolecular metal‐organic complexes of Fe 3+ and tannic acid were used as an eco‐friendly immobilization technique for ω‐Ta binding. The immobilized enzyme maintained the optimal pH, temperature, and storage stability as the soluble enzyme. The immobilized enzyme showed good reusability, retaining over 50% of its initial activity after five cycles. The utility of the modified support was also demonstrated for one‐step purification and immobilization of the enzyme. These results demonstrate a straightforward, economical, and environmentally benign approach to enzyme immobilization for industrial application.

Chemistry - MethodsVol. 6(5)
Institute of Molecular Medicine (IN), Indian Institute of Technology Delhi (IN)
Responsible consumption and production
Openalex Percentile: Top 7%
Enzyme Catalysis and Immobilization
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