Characterization and application of d-amino acid oxidase and catalase within permeabilized Pichia pastoris cells in bioconversions

Tan, Qiang; Song, Qing; Zhang, Ye-Wang; Wei, Dongzhi

doi:10.1007/s12010-007-9026-6

Cited by 21 publications

(17 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

View full text Add to dashboard Cite

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“…D-Amino acid deaminases from many yeasts, including Trigonopsis variabilis (Brodelius et al 1981), Rhodotorula gracilis (Butò et al 1994), and Pichia pastoris (Tan et al 2007), have been used to produce PPA. However, their substrate, D-phenylalanine, is expensive and unfavorable for large-scale industrial PPA production.…”

Section: Introductionmentioning

confidence: 99%

Production of phenylpyruvic acid from l-phenylalanine using an l-amino acid deaminase from Proteus mirabilis: comparison of enzymatic and whole-cell biotransformation approaches

Hou

Hossain

et al. 2015

Appl Microbiol Biotechnol

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Phenylpyruvic acid (PPA) is an important organic acid that has a wide range of applications. In this study, the membrane-bound L-amino acid deaminase (L-AAD) gene from Proteus mirabilis KCTC 2566 was expressed in Escherichia coli BL21(DE3) and then the L-AAD was purified. After that, we used the purified enzyme and the recombinant E. coli whole-cell biocatalyst to produce PPA via a one-step biotransformation from L-phenylalanine. L-AAD was solubilized from the membrane and purified 52-fold with an overall yield of 13 %, which corresponded to a specific activity of 0.94 ± 0.01 μmol PPA min(-1)·mg(-1). Then, the biotransformation conditions for the pure enzyme and the whole-cell biocatalyst were optimized. The maximal production was 2.6 ± 0.1 g·L(-1) (specific activity of 1.02 ± 0.02 μmol PPA min(-1)·mg(-1) protein, 86.7 ± 5 % mass conversion rate, and 1.04 g·L(-1)·h(-1) productivity) and 3.3 ± 0.2 g L(-1) (specific activity of 0.013 ± 0.003 μmol PPA min(-1)·mg(-1) protein, 82.5 ± 4 % mass conversion rate, and 0.55 g·L(-1)·h(-1) productivity) for the pure enzyme and whole-cell biocatalyst, respectively. Comparative studies of the enzymatic and whole-cell biotransformation were performed in terms of specific activity, production, conversion, productivity, stability, need of external cofactors, and recycling. We have developed two eco-friendly and efficient approaches for PPA production. The strategy described herein may aid the biotransformational synthesis of other α-keto acids from their corresponding amino acids.

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“…Another important application of this “oxidase–catalase” oxidation system is the deamination of α‐amino acid substrates into the corresponding α‐keto acids mediated by d ‐amino acid oxidase (DAO, EC 1.4.3.3), which has many applications such as the production of α‐keto acids, 7‐aminocephalosporanic acid (7‐ACA), and resolution of racemic mixtures of amino acids . Tan et al reported high‐density fermentation of a recombinant P. pastoris strain coexpressed with DAO and catalase. The activities of the two enzymes with the permeabilized cells reached 12 532 and 684 800 U L −1 and exhibited relatively high stability.…”

Section: P Pastoris As a Whole‐cell Biocatalystmentioning

confidence: 99%

Pichia pastoris as a Versatile Cell Factory for the Production of Industrial Enzymes and Chemicals: Current Status and Future Perspectives

Zhu

Sun

2019

Biotechnology Journal

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With nearly three decades of development, Pichia pastoris (P. pastoris) has become a powerful eukaryotic protein expression system for the expression of thousands of proteins both on a laboratory and industrial scale. In addition, it has also been extensively used as a cell factory for the production of a variety of chemicals. This review summarizes the bottlenecks and solutions in achieving high-level secretory protein expression with P. pastoris and then outlines its applications on chemical production with an emphasis on its role as whole-cell biocatalyst. Furthermore, current challenges and future directions of this important system are also discussed.

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Characterization and application of d-amino acid oxidase and catalase within permeabilized Pichia pastoris cells in bioconversions

Cited by 21 publications

References 17 publications

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Hydrogen Peroxide in Biocatalysis. A Dangerous Liaison

Production of phenylpyruvic acid from l-phenylalanine using an l-amino acid deaminase from Proteus mirabilis: comparison of enzymatic and whole-cell biotransformation approaches

Pichia pastoris as a Versatile Cell Factory for the Production of Industrial Enzymes and Chemicals: Current Status and Future Perspectives

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