The coimmobilization of d-amino acid oxidase and catalase enables the quantitative transformation of d-amino acids (d-phenylalanine) into α-keto acids (phenylpyruvic acid)

Fernández‐Lafuente, Roberto; Rodríguez, Verónica; Guisán, José M.

doi:10.1016/s0141-0229(98)00028-3

Cited by 142 publications

(94 citation statements)

References 17 publications

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“…Thus, oxidase and catalase co-immobilization proved to be the most effective way to prevent accumulation of hydrogen peroxide ( Figure 2), even though co-immobilization of several enzymes may raise some problems, it became necessary in this particular case [162]. This strategy has been established in the production of other alphaketo acids [163][164][165][166][167]. Moreover, the catalase-D-amino acid oxidase system has been used in the determination of racemized aminoacid after alkali treatment of proteins [168].…”

Section: +mentioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

COC

137

107

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Hydrogen peroxide is a substrate or side-product in many enzyme-catalyzed reactions. For example, it is a side-product of oxidases, resulting from the re-oxidation of FAD with molecular oxygen, and it is a substrate for peroxidases and other enzymes. However, hydrogen peroxide is able to chemically modify the peptide core of the enzymes it interacts with, and also to produce the oxidation of some cofactors and prostetic groups (e.g., the hemo group). Thus, the development of strategies that may permit to increase the stability of enzymes in the presence of this deleterious reagent is an interesting target. This enhancement in enzyme stability has been attempted following almost all available strategies: site-directed mutagenesis (eliminating the most reactive moieties), medium engineering (using stabilizers), immobilization and chemical modification (trying to generate hydrophobic environments surrounding the enzyme, to confer higher rigidity to the protein or to generate oxidation-resistant groups), or the use of systems capable of decomposing hydrogen peroxide under very mild conditions. If hydrogen peroxide is just a side-product, its immediate removal has been reported to be the best solution. In some cases, when hydrogen peroxide is the substrate and its decomposition is not a sensible solution, researchers coupled one enzyme generating hydrogen peroxide "in situ" to the target enzyme resulting in a continuous supply of this reagent at low concentrations thus preventing enzyme inactivation.This review will focus on the general role of hydrogen peroxide in biocatalysis, the main mechanisms of enzyme inactivation produced by this reactive and the different strategies used to prevent enzyme inactivation caused by this "dangerous liaison". Outlook

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Section: +mentioning

confidence: 99%

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hernández

Berenguer-Murcia²,

Rodrigues³

et al. 2012

COC

137

107

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“…In addition to its crucial biological relevance, this enzyme has many industrial applications, including (i) degradation of hydrogen peroxide after textile bleaching in order to prevent problems in subsequent dyeing (12); (ii) in the dairy industry, elimination of H 2 O 2 added to sterilize milk (2, 44); (iii) coupled with oxidases, prevention of inactivation of the oxidases in the presence of high peroxide concentrations (15,23,43); and (iv) coupled with oxidases, prevention of the destruction by H 2 O 2 of the target product in an oxidase-catalyzed reaction (19,42).…”

mentioning

confidence: 99%

Thermus thermophilus as a Cell Factory for the Production of a Thermophilic Mn-Dependent Catalase Which Fails To Be Synthesized in an Active Form in Escherichia coli

Hidalgo

Betancor

Moreno

et al. 2004

Appl Environ Microbiol

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Thermostable Mn-dependent catalases are promising enzymes in biotechnological applications as H 2 O 2 -detoxifying systems. We cloned the genes encoding Mn-dependent catalases from Thermus thermophilus HB27 and HB8 and a less thermostable mutant carrying two amino acid replacements (M129V and E293G). When the wild-type and mutant genes were overexpressed in Escherichia coli, unmodified or six-His-tagged proteins of the expected size were overproduced as inactive proteins. Several attempts to obtain active forms or to activate the overproduced proteins were unsuccessful, even when soluble and thermostable proteins were used. Therefore, a requirement for a Thermus-specific activation factor was suggested. To overcome this problem, the Mn-dependent catalase genes were overexpressed directly in T. thermophilus under the control of the Pnar promoter. This promoter belongs to a respiratory nitrate reductase from of T. thermophilus HB8, whose transcription is activated by the combined action of nitrate and anoxia. Upon induction in T. thermophilus HB8, a 20-to 30-fold increase in catalase specific activity was observed, whereas a 90-to 110-fold increase was detected when the laboratory strain T. thermophilus HB27::nar was used as the host. The thermostability of the overproduced wild-type catalase was identical to that previously reported for the native enzyme, whereas decreased stability was detected for the mutant derivative. Therefore, our results validate the use of T. thermophilus as an alternative cell factory for the overproduction of thermophilic proteins that fail to be expressed in well-known mesophilic hosts.Catalases (EC 1.11.1.6) are widely distributed enzymes in nature that decompose hydrogen peroxide to water and molecular oxygen as a detoxifying mechanism. In addition to its crucial biological relevance, this enzyme has many industrial applications, including (i) degradation of hydrogen peroxide after textile bleaching in order to prevent problems in subsequent dyeing (12); (ii) in the dairy industry, elimination of H 2 O 2 added to sterilize milk (2, 44); (iii) coupled with oxidases, prevention of inactivation of the oxidases in the presence of high peroxide concentrations (15,23,43); and (iv) coupled with oxidases, prevention of the destruction by H 2 O 2 of the target product in an oxidase-catalyzed reaction (19,42).

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“…However, as noticed by other authors 16 , a comprehensive analysis of operational stability of immobilized enzyme is most often missing. Thus, in this report the authors have focused on this topic, and not on the optimization of the immobilization procedure itself, although some groups of authors reported thorough studies on stability of immobilized enzyme 6,15,17,18 . DAAO was immobilized on Eupergit C in this work.…”

Section: Stabilization Of D-amino Acid Oxidase Via Covalent Immobilizmentioning

confidence: 99%

Stabilization of D-Amino Acid Oxidase via Covalent Immobilization and Mathematical Model of D-Methionine Oxidative Deamination Catalyzed by Immobilized Enzyme

Findrik

Tusić

Vasić-Rački

2016

Chem.Biochem.Eng.Q.

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Prigorje Brdovečko, Croatia (current position)Porcine kidney D-amino acid oxidase was stabilized by covalent immobilization on spherical particles of Eupergit C because of its low stability in soluble form. The focus of this work was to evaluate operational stability of the immobilized enzyme. To evaluate D-amino acid oxidase's operational stability during process conditions, repetitive batch reactor experiments of D-methionine oxidation reaction were carried out with continuous aeration for oxygen supply at air-flow rates of 5 and 10 dm 3 h -1 . Kinetic analysis of the immobilized enzyme was done as well. The mathematical model of D-methionine oxidative deamination catalyzed by the immobilized D-amino acid oxidase was developed and it described the data well. It enabled the estimation of operational stability decay rate constant. It was possible to achieve 100 % substrate conversion in all batch experiments.

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The coimmobilization of d-amino acid oxidase and catalase enables the quantitative transformation of d-amino acids (d-phenylalanine) into α-keto acids (phenylpyruvic acid)

Cited by 142 publications

References 17 publications

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Thermus thermophilus as a Cell Factory for the Production of a Thermophilic Mn-Dependent Catalase Which Fails To Be Synthesized in an Active Form in Escherichia coli

Stabilization of D-Amino Acid Oxidase via Covalent Immobilization and Mathematical Model of D-Methionine Oxidative Deamination Catalyzed by Immobilized Enzyme

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