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

Li, Rong; Sun, Jian; Fu, Yaqi; Du, Kun; Cai, Mengsha; Ji, Peijun; Feng, Wei

doi:10.3390/catal6050066

Cited by 12 publications

(8 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Traditionally, enzyme recycling is handled through their immobilization. Such technology is well developed for single enzymes but is not as advanced for enzyme cascades [7][8][9][10][11][12][13][14][15]. Commonly, the immobilization of enzyme ensembles can be achieved by their separate immobilization on individual support particles or by the co-immobilization of all the enzymes on the same support.…”

Section: Introductionmentioning

confidence: 99%

Co-Immobilization of D-Amino Acid Oxidase, Catalase, and Transketolase for One-Pot, Two-Step Synthesis of L-Erythrulose

et al. 2023

View full text Add to dashboard Cite

Here, we present an immobilized enzyme cascade in a basket-type reactor allowing a one-pot, two-step enzymatic synthesis of L-erythrulose from D-serine and glycolaldehyde. Three enzymes, D-amino acid oxidase from Rhodotorula gracilis (DAAORg), catalase from bovine liver (CAT), and transketolase from Geobacillus stearothermophilus (TKgst) were covalently immobilized on silica monolithic pellets, characterized by an open structure of interconnected macropores and a specific surface area of up to 300 m2/g. Three strategies were considered: (i) separate immobilization of enzymes on silica supports ([DAAO][CAT][TK]), (ii) co-immobilization of two of the three enzymes followed by the third ([DAAO+CAT][TK]), and (iii) co-immobilization of all three enzymes ([DAAO+CAT+TK]). The highest L-erythrulose concentrations were observed for the co-immobilization protocols (ii) and (iii) (30.7 mM and 29.1 mM, respectively). The reusability study showed that the best combination was [DAAO + CAT][TK], which led to the same level of L-erythrulose formation after two reuse cycles. The described process paves the way for the effective synthesis of a wide range of α-hydroxyketones from D-serine and suitable aldehydes.

show abstract

Section: Introductionmentioning

confidence: 99%

Co-Immobilization of D-Amino Acid Oxidase, Catalase, and Transketolase for One-Pot, Two-Step Synthesis of L-Erythrulose

et al. 2023

View full text Add to dashboard Cite

show abstract

“…In some instances, e.g., when the product of the first enzyme is unstable [55,84,85], co-immobilization is the only way to obtain a high yield of the desired product since even a short time might permit its modification of another undesired compound. Several cases of this kind of cascade have also been reported in the scientific literature [86][87][88][89][90][91].…”

Section: Introductionmentioning

confidence: 87%

“…Another case is when the rapid and efficient action of the second enzyme is critical to prevent the modification of the product. This is the case of an intrinsically unstable intermediate product or the production of a reactive by-product (e.g., hydrogen peroxide) able to destroy the target product [86][87][88][89][90][91]. In this case, the inactivation of the first enzyme may have a similar effect to the above case.…”

Section: Long-term Performance Of a Combi-biocatalyst Using Enzymes W...mentioning

confidence: 99%

Co-Enzymes with Dissimilar Stabilities: A Discussion of the Likely Biocatalyst Performance Problems and Some Potential Solutions

et al. 2022

View full text Add to dashboard Cite

Enzymes have several excellent catalytic features, and the last few years have seen a revolution in biocatalysis, which has grown from using one enzyme to using multiple enzymes in cascade reactions, where the product of one enzyme reaction is the substrate for the subsequent one. However, enzyme stability remains an issue despite the many benefits of using enzymes in a catalytic system. When enzymes are exposed to harsh process conditions, deactivation occurs, which changes the activity of the enzyme, leading to an increase in reaction time to achieve a given conversion. Immobilization is a well-known strategy to improve many enzyme properties, if the immobilization is properly designed and controlled. Enzyme co-immobilization is a further step in the complexity of preparing a biocatalyst, whereby two or more enzymes are immobilized on the same particle or support. One crucial problem when designing and using co-immobilized enzymes is the possibility of using enzymes with very different stabilities. This paper discusses different scenarios using two co-immobilized enzymes of the same or differing stability. The effect on operational performance is shown via simple simulations using Michaelis–Menten equations to describe kinetics integrated with a deactivation term. Finally, some strategies for overcoming some of these problems are discussed.

show abstract

“…Recently, Feng and coworkers modified a d -amino acid oxidase (DAAO) and CAT by fusing them with an elastin-like polypeptide (ELP). Then ELP-DAAO and ELP-CAT were immobilized on multiwalled carbon nanotubes to realize H 2 O 2 decomposition . Afterward, the same group developed a specific ligation of the N-terminus of the DAAO subunits and the C-terminus of the CAT subunits with native peptides through intein-mediated protein splicing for the decomposition of the generated H 2 O 2 .…”

Section: Introductionmentioning

confidence: 99%

“…Then ELP-DAAO and ELP-CAT were immobilized on multiwalled carbon nanotubes to realize H 2 O 2 decomposition. 9 Afterward, the same group developed a specific ligation of the N-terminus of the DAAO subunits and the C-terminus of the CAT subunits with native peptides through intein-mediated protein splicing for the decomposition of the generated H 2 O 2 . 10 Although the multienzyme system favors efficient H 2 O 2 decomposition and α-keto acid synthesis, the intrinsic drawbacks of natural enzymes, such as high cost, limited stability, poor reusability, and the time-consuming separation and purification, greatly restrain their extensive application in large-scale production.…”

mentioning

confidence: 99%

Cobalt Phosphate Nanocrystals: A Catalase-Like Nanozyme and In Situ Enzyme-Encapsulating Carrier for Efficient Chemoenzymatic Synthesis of α-Keto Acid

Wang

Liu

Dong

et al. 2021

ACS Appl. Mater. Interfaces

View full text Add to dashboard Cite

Chemoenzymatic catalysis combining the traits of chemical and enzymatic catalysis provides tremendous possibilities for the design of biosynthetic pathways utilizing inorganic catalysts and enzymes. However, the efficiency of chemoenzymatic catalysis is usually governed by the synergy and compatibility of the two catalysts. Here, we report for the first time the catalase-like activity of cobalt phosphate nanocrystals (CoPs). By a one-pot biomimetic mineralization with CoPs and L-amino acid oxidase (LAAO) under a mild condition, we have fabricated a hybrid nanobiocatalyst, LAAO@CoPs, for the chemoenzymatic synthesis of α-keto acid. The as-fabricated nanobiocatalyst with directly contacted catalytic sites of the enzyme and nanozyme maximizes the substrate channeling effects for in situ chemical decomposition of the oxidative intermediate, H 2 O 2 , during the enzymatic oxidation of L-tryptophan (L-Trp), thus minimizing the H 2 O 2 accumulation and byproduct generation. Benefiting from the superiority of LAAO@CoPs, complete conversion (100.0%) of L-Trp to indole pyruvic acid is achieved, over two times higher than the yield of the free LAAO system (47.6%). Meanwhile, LAAO@ CoPs show high stabilities against heat and proteolytic treatments. This work offers a new design approach for constructing a highperformance nanobiocatalyst for cascade reactions, especially for those systems with toxic or reactive intermediates.

show abstract

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

Cited by 12 publications

References 35 publications

Co-Immobilization of D-Amino Acid Oxidase, Catalase, and Transketolase for One-Pot, Two-Step Synthesis of L-Erythrulose

Co-Immobilization of D-Amino Acid Oxidase, Catalase, and Transketolase for One-Pot, Two-Step Synthesis of L-Erythrulose

Co-Enzymes with Dissimilar Stabilities: A Discussion of the Likely Biocatalyst Performance Problems and Some Potential Solutions

Cobalt Phosphate Nanocrystals: A Catalase-Like Nanozyme and In Situ Enzyme-Encapsulating Carrier for Efficient Chemoenzymatic Synthesis of α-Keto Acid

Contact Info

Product

Resources

About