Enhancement of the solubility and stability of d-amino acid oxidase by fusion to an elastin like polypeptide

Du, Kun; Sun, Jian; Song, Xiaoqiang; Song, Cuidan; Feng, Wei

doi:10.1016/j.jbiotec.2015.07.016

Cited by 12 publications

(19 citation statements)

References 45 publications

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“…All other reagents were purchased from Sinopharm Chemical Reagent Co., Ltd (Shanghai, China) or Sigma-Aldrich (Shanghai, China) and used without additional purification processes. Elastin-like polypeptide (ELP), modified D-Amino acid oxidase, and catalase were expressed and purified as described in our previous work [27]. The expression vector pET28a/(VPGXG) 60 -CAT in Escherichia coli was constructed.…”

Section: Methodsmentioning

confidence: 99%

“…Two-enzyme systems with different weight ratios of ELP-CAT/O-MWNTs to ELP-ELP/O-MWNTs were investigated. Figure 6 shows the results, in which the specific activity ratio is defined as the ratio of the specific activity of the immobilized enzymes to the specific activity of ELP-DAAO (0.21 U/mg) [27]. Obviously, a larger specific activity ratio means a higher specific activity.…”

Section: Enzymatic Catalysismentioning

confidence: 99%

“…In previous work, D-amino acids oxidase was genetically modified by fusing it to an elastin-like polypeptide (ELP) [27]. In this work, catalase (CAT) was fused to ELP through genetic engineering technology.…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of Genetically-Modified d-Amino Acid Oxidase and Catalase on Carbon Nanotubes to Improve the Catalytic Efficiency

Sun

et al. 2016

Catalysts

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D-amino acid oxidase (DAAO) and catalase (CAT) have been genetically modified by fusing them to an elastin-like polypeptide (ELP). ELP-DAAO and ELP-CAT have been separately immobilized on multi-walled carbon nanotubes (MWNTs). It has been found that the secondary structures of the enzymes have been preserved. ELP-DAAO catalyzed the oxidative deamination of D-alanine, and H 2 O 2 was evolved continuously. When the MWNT-supported enzymes were used together, the generated hydrogen peroxide of ELP-DAAO could be decomposed in situ. The catalytic efficiency of the two immobilized enzymes was more than five times greater than that of free ELP-DAAO when the ratio of immobilized ELP-CAT to immobilized ELP-DAAO was larger than 1:1.

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Section: Methodsmentioning

confidence: 99%

Section: Enzymatic Catalysismentioning

confidence: 99%

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Immobilization of Genetically-Modified d-Amino Acid Oxidase and Catalase on Carbon Nanotubes to Improve the Catalytic Efficiency

Sun

et al. 2016

Catalysts

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“…Surfaces coated with an ELP fused to the RGD or fibronectin CS5 cell binding sequence retained the ability to support in vitro endothelial cell adhesion and spreading[79]. Additional uses of ELPs include purification of holoenzymes such as D-Amino acid oxidase [80], isolation of multisubunit enzymes like RNA polymerase [81], entrapment of small molecules[66], and the generation of ELPs hybridized with other polymers [71]. …”

Section: Introductionmentioning

confidence: 99%

Elastin-like polypeptides: Therapeutic applications for an emerging class of nanomedicines

Despanie

Dhandhukia

Hamm‐Alvarez

et al. 2016

Journal of Controlled Release

129

104

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Elastin-like polypeptides (ELPs) constitute a genetically engineered class of ‘protein polymers’ derived from human tropoelastin. They exhibit a reversible phase separation whereby samples remain soluble below a transition temperature (Tt) but form amorphous coacervates above Tt. Their phase behavior has many possible applications in purification, sensing, activation, and nanoassembly. As humanized polypeptides, they are non-immunogenic, substrates for proteolytic biodegradation, and can be decorated with pharmacologically active peptides, proteins, and small molecules. Recombinant synthesis additionally allows precise control over ELP architecture and molecular weight, resulting in protein polymers with uniform physicochemical properties suited to the design of multifunctional biologics. As such, ELPs have been employed for various uses including as anti-cancer agents, ocular drug delivery vehicles, and protein trafficking modulators. This review aims to offer the reader a catalogue of ELPs, their various applications, and potential for commercialization across a broad spectrum of fields.

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“…Recently, there are many researchesinvestigating strategies on improving the solubility of crystal compound such as additives effect 1,3 , cocrystal formation 4 , solvent effect 5 and thermal effect 6 .Amino acids are one of simple biomolecules and are an important building block of native protein. Due to their importance in many industrial applications such as food and pharmaceutical sectors, many researchers are interested on the solubility enhancement 7,8 as well as the thermodynamic properties of amino acids 9 . Therefore, in this work, L-alanine was selected as the model compound, in which it is classified as a nonessential aliphatic amino acid which contains a methyl group 10 .…”

Section: Introductionmentioning

confidence: 99%

Influence of amino acid additives on solution behaviour of L-alanine

Othman

Anuar

Bakar

et al. 2018

Chem. Eng. Res. Bull.

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Abstract:The solubility experiment of L-alanine solution was performed in a 250ml jacketed glass crystallizer without and with amino acid additives at temperature from 15 o C to 75 o C by means of gravimetric method. On the whole, L-leucine additive significantly altered the solubility of L-alanine and Glycine additive caused an erratic pattern on the solubility data of L-alanine. The hydrophobic methyl side chain of L-leucine additives is believed to contribute to the formation of water clathrate in the solution which affected the interaction of L-alanine molecules in water solvent and thus modified the solubility of L-alanine. Finally, thermodynamic data analysis of L-alanine solution was extensively assessed. The negative deviation of L-alanine from the ideal solution is as a result of high solute-solvent interaction, which is due to the hydrophobicity and clathrate phenomenon of the water molecules in the solution.

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Enhancement of the solubility and stability of d-amino acid oxidase by fusion to an elastin like polypeptide

Cited by 12 publications

References 45 publications

Immobilization of Genetically-Modified d-Amino Acid Oxidase and Catalase on Carbon Nanotubes to Improve the Catalytic Efficiency

Immobilization of Genetically-Modified d-Amino Acid Oxidase and Catalase on Carbon Nanotubes to Improve the Catalytic Efficiency

Elastin-like polypeptides: Therapeutic applications for an emerging class of nanomedicines

Influence of amino acid additives on solution behaviour of L-alanine

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