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Updated: Feb 11, 2026

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
Published on: April 22, 2016
Novel Biocatalysts by Chemical Modification of Known Enzymes: Cross-Linked Microcrystals of the Semisynthetic
Dietmar Häring1, Peter Schreier1
1Lehrstuhl für Lebensmittelchemie der Universität, Am Hubland, D-97074 Würzburg (Germany), Fax: (+49) 931-888-5484.
Abstract:
The linkage of lysine residues on the surfaces of subtilisin crystals (NH2 -Enz; see Scheme) with glutardialdehyde affords an immobilized biocatalyst of high stability and purity. The replacement of the serine OH group in the active site (Enz-OH) by SeO2 H leads to new activity as a peroxidase. Thus for the first time, chemical enzyme engineering has resulted in a biocatalyst with a modified peptide framework as well as a new catalytically active site. This methodology combines reasonable substrate selectivity of a semisynthetic enzyme with the exceptional stability of cross-linked enzyme crystals.
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