NDLI: Immobilization of l-aspartate oxidase from <i>Sulfolobus tokodaii</i> as a biocatalyst for resolution of aspartate solutions

Content Provider	Royal Society of Chemistry (RSC)
Author	Tessaro, Davide Piubelli, Luciano Rosini, Elena Valentino, Mattia D'Arrigo, Paola Allegretti, Chiara Fiorati, Andrea Pollegioni, Loredano
Copyright Year	2015
Abstract	L-Aspartate oxidase from the thermophilic archaebacterium Sulfolobus tokodaii (StLASPO) catalyzes the stereoselective oxidative deamination of L-aspartate to yield oxaloacetate, ammonia and hydrogen peroxide. The recombinant flavoenzyme shows distinctive features that make it attractive for biotechnological applications (it is highly thermostable, it is stable in a broad pH range, it tightly binds the FAD cofactor and it shows a low Km for dioxygen). In order to set up an efficient and economically feasible bioconversion process, in this work, we investigated the immobilization of this novel biocatalyst. The best results in terms of immobilization yield have been obtained when StLASPO was immobilized on the amino support Relizyme™ HA403/S R after activation with glutaraldehyde and on the epoxy support SEPABEADS® EC-EP/S (in both cases, through the free amino groups of the enzyme), as well as prepared as cross-linked enzyme aggregates (CLEA). By using the Relizyme™ HA403/S R support, as well as by the CLEA preparation procedure, full immobilization in terms of enzymatic activity was obtained. Immobilized StLASPO was used for the resolution of racemic solutions of 50 mM D,L-aspartate achieving full resolution in <1 hour. Indeed, the Relizyme-StLASPO immobilized enzyme (the one showing the highest immobilization yield) was efficiently reused in 5 cycles keeping full oxidation of L-aspartate in ≤2 hours. In a semi-preparative scale reaction, 66 mg of enantiomerically pure D-aspartate were produced in 1 day using 20 units of enzyme.
Starting Page	1106
Ending Page	1114
Page Count	9
File Format	HTM / HTML PDF
ISSN	20444753
Volume Number	5
Issue Number	2
Journal	Catalysis Science & Technology
DOI	10.1039/c4cy00968a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Oxygen Hydrogen peroxide Enzyme Archaea Oxidase Cofactor (biochemistry) Sulfolobus Oxaloacetic acid Stereoselectivity Ammonia Racemic mixture Glutaraldehyde Thermophile Oxidative deamination Epoxide CLEA Aspartic acid Vrije Universiteit Brussel Catalysis Flavin adenine dinucleotide Immobilized enzyme
Content Type	Text
Resource Type	Article
Subject	Catalysis

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