Immobilization of formate dehydrogenase on polyethylenimine‐grafted graphene oxide with kinetics and stability study

Lin, Peng; Zhang, Yonghui; Yao, Guangxiao; Huo, Heyu; Ren, Hong; Wang, Yixuan; Wang, Shizhen; Fang, Baishan

doi:10.1002/elsc.201900134

Cited by 30 publications

(12 citation statements)

References 29 publications

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“…Furthermore, the encapsulation efficiency did not change substantially regardless of the concentration of input enzymes (Figures S4c and S4d). Considering that typical enzyme loading capacities are few hundreds mg/g, ,− the enzyme loading capacity of the PNC seems very high. Since the loading capacity is often related to the physical structure of the PNC rather than the type of enzyme, we evaluated the loading of two enzymes as representative cases.…”

Section: Resultsmentioning

confidence: 99%

“…Yeast extract, tryptone, and agar were obtained from DB Biosciences (San Jose, CA, USA). Pluronic F127, poly(ethylene oxide) 100 -poly-(propylene oxide) 65 -poly(ethylene oxide) 100 (PEO-PPO-PEO) copolymer (MW: 12.6 kDa), was kindly donated by BASF Corporation (Seoul, South Korea). Acryloyl chloride was bought from Tokyo Chemical Industry (Tokyo, Japan).…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

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Pluronic-Based Nanocarrier Platform Encapsulating Two Enzymes for Cascade Reactions

Kim

Kwon

Cha

et al. 2020

ACS Appl. Bio Mater.

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Enzyme immobilization is very important for diverse enzyme applications. Particularly, there is a growing need for coimmobilization of multiple enzymes for biosensing and synthetic applications. However, it is still challenging to coimmobilize two enzymes with desirable features, including high immobilization yield, retention of enzymatic activity, and low leaching. In this study, we demonstrated that a pluronic-based nanocarrier (PNC) can be an encapsulation platform for immobilization of various single enzymes. Since the PNC is temperature-sensitive, a simple temperature change from 4 to 37 °C led to a substantial size reduction and enzyme encapsulation. All six enzymes tested were encapsulated by the PNC in high yield (∼90%) with the retained enzymatic activity (>95%). The leaching of encapsulated enzymes was very minimal (<0.13% for 2 weeks). Then, we demonstrated that the PNC can efficiently coencapsulate two enzymes, formate dehydrogenase (FDH) and mannitol dehydrogenase (MDH), for a cascade reaction producing d-mannitol. Coencapsulation of FDH and MDH resulted in an over 10-fold increase in d-mannitol production compared to the free mix of FDH and MDH, likely due to the enhanced local concentrations of FDH and MDH inside the PNC.

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Section: Resultsmentioning

confidence: 99%

Section: ■ Materials and Methodsmentioning

confidence: 99%

Pluronic-Based Nanocarrier Platform Encapsulating Two Enzymes for Cascade Reactions

Kim

Kwon

Cha

et al. 2020

ACS Appl. Bio Mater.

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“…B-PEI has many potential applications due to its polycationic character and water solubility [ 3 , 4 , 5 ]. In biomedical applications, it has been used as an additive to improve the specificity and efficiency of the polymerase chain reaction (PCR) for DNA amplification [ 6 ]; enzyme immobilization [ 7 , 8 ]; construction of biosensors [ 9 , 10 ]; drug delivery [ 11 , 12 ] and gene therapy [ 13 , 14 ]. For the last application, b-PEI with a molecular weight of 25 kDa has been reported as one of the polymers most used as a non-viral vector for the transport of nucleic acids due to its ability to form polyplexes with nucleic acids through electrostatic interactions between the amino groups of b-PEI and the phosphate groups of nucleic acids [ 15 , 16 , 17 ].…”

Section: Introductionmentioning

confidence: 99%

Modification of Branched Polyethyleneimine Using Mesquite Gum for Its Improved Hemocompatibility

et al. 2021

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In the present study, the modification of branched polyethyleneimine (b-PEI) was carried out using mesquite gum (MG) to improve its hemocompatibility to be used in biomedical applications. In the copolymer synthesis process (carboxymethylated mesquite gum grafted polyethyleneimine copolymer (CBX-MG-PEI), an MG carboxymethylation reaction was initially carried out (carboxymethylated mesquite gum (CBX-MG). Subsequently, the functionalization between CBX-MG and b-PEI was carried out using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) and N-hydroxysuccinimide (NHS) as crosslinking agents. The synthesis products were characterized using Fourier transform infrared spectroscopy (FTIR), X-ray photoelectron spectroscopy (XPS), and thermogravimetric analysis (TGA). Thermogravimetric analysis showed that CBX-MG and CBX-MG-PEI presented a lower decomposition temperature than MG. The CBX-MG-PEI has a high buffer capacity in the pH range of 4 to 7, similar to the b-PEI. In addition, the CBX-MG-PEI showed an improvement in hemocompatibility in comparison with the b-PEI. The results showed a non-hemolytic property at doses lower than 0.1 µg/mL (CBX-MG-PEI). These results allow us to propose that this copolymer be used in transfection, polymeric nanoparticles, and biomaterials due to its physicochemical and hemocompatibility properties.

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“…Materials like carbon nanotubes (CNTs), graphene oxides (GO) and metal organic frameworks (MOFs) enable stable and high-density enzyme-immobilization, high activity and easy regeneration [3]. Lin et al used GO-based nanomaterials for immobilizing formate dehydrogenase observing high stability and recovery yield ensuring a high grade of reusability [4]. Ji et al immobilized laccase on a polymeric membrane coating of CNTs using electrostatic interaction.…”

Section: Introductionmentioning

confidence: 99%

“…Lin et al. used GO‐based nanomaterials for immobilizing formate dehydrogenase observing high stability and recovery yield ensuring a high grade of reusability [ 4 ]. Ji et al.…”

Section: Introductionmentioning

confidence: 99%

A versatile ceramic capillary membrane reactor system for continuous enzyme‐catalyzed hydrolysis

Messner

Antink

Guo

et al. 2021

Engineering in Life Sciences

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As an alternative to classical batch processes, enzyme-catalyzed hydrolysis can also be carried out continuously. To facilitate this, a continuous ceramic capillary membrane reactor system (CCCMRS) was developed which can be operated with various proteolytic enzymes immobilized on the porous ceramic capillary membranes. This system has several advantages over common batch processes regarding stability, reproducibility and controllability and can easily be adapted to optimal reaction conditions and individual preferences. Two exemplary applications utilizing the CCCMRS were carried out and investigated in long-term stability studies. In the first application the continuous enzymatic cleavage of human IgG into the antibody fragments Fab and Fc by immobilized papain was performed. A total volume of 22 mL of 1 mg mL -1 IgG-solution was enzymatically cleaved over a period of 33.3 h. The antibody cleavage products could be detected in an SEC-HPLC over the whole process time thus indicating long-term stability of the continuous hydrolysis process. The second application investigated the continuous digestion of pea and almond protein isolates by immobilized Alcalase resulting in the generation of a large variety of different peptides. This peptide fingerprint remains constant over a long period of time enabling fractionation and thus making the peptides accessible for further bioactivity studies in sufficient quantities. The constant peptide fingerprint could be shown in the RP-HPLC analysis for all 30 samples with a total volume of 29.7 mL collected over a period of 45 h.

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Immobilization of formate dehydrogenase on polyethylenimine‐grafted graphene oxide with kinetics and stability study

Cited by 30 publications

References 29 publications

Pluronic-Based Nanocarrier Platform Encapsulating Two Enzymes for Cascade Reactions

Pluronic-Based Nanocarrier Platform Encapsulating Two Enzymes for Cascade Reactions

Modification of Branched Polyethyleneimine Using Mesquite Gum for Its Improved Hemocompatibility

A versatile ceramic capillary membrane reactor system for continuous enzyme‐catalyzed hydrolysis

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