Preparation of a Flower-Like Immobilized D-Psicose 3-Epimerase with Enhanced Catalytic Performance

Zheng, Lu; Sun, Yining; Wang, Jing; Huang, He; Geng, Xin; Tong, Yi; Wang, Zhi

doi:10.3390/catal8100468

Cited by 39 publications

(14 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, the highest activity recovery was obtained with HNFs prepared with 0.16 M phosphate buffer and 30 mM CoCl 2 . In a study by Zheng et al 40 , D-psicose 3-epimerase (DPEase)@Co 3 (PO 4 ) 2 •HNFs were prepared by incubation of a solution containing Co 2+ (1.9 mM), phosphate buffer (50 mM, pH 7.5), and DPEase (1 mg mL −1 ) at 4 °C for 48 h. In another study, cellobiose 2-epimerase (mutant E161D/N365P) (EDNP)@Co 3 (PO 4 ) 2 •HNFs were obtained by the addition of CoCl 2 to PBS (10 mM, pH 7.4) and incubation of the mixture for 24 h at room temperature 41 . The activity recovery was increased with the Co 2+ concentration in the synthesis mixture, and the highest activity recovery was achieved at 2 mM Co 2+ .…”

Section: Resultsmentioning

confidence: 98%

Instantaneous synthesis and full characterization of organic–inorganic laccase-cobalt phosphate hybrid nanoflowers

Vojdanitalab

Jafari-Nodoushan

Mojtabavi

et al. 2022

Sci Rep

View full text Add to dashboard Cite

A novel approach termed the "concentrated method" was developed for the instant fabrication of laccase@Co3(PO4)2•hybrid nanoflowers (HNFs). The constructed HNFs were obtained by optimizing the concentration of cobalt chloride and phosphate buffer to reach the highest activity recovery. The incorporation of 30 mM CoCl2 and 160 mM phosphate buffer (pH 7.4) resulted in a fast anisotropic growth of the nanomaterials. The purposed method did not involve harsh conditions and prolonged incubation of precursors, as the most reported approaches for the synthesis of HNFs. The catalytic efficiency of the immobilized and free laccase was 460 and 400 M−1S−1, respectively. Also, the enzymatic activity of the prepared biocatalyst was 113% of the free enzyme (0.5 U mL−1). The stability of the synthesized HNFs was enhanced by 400% at pH 6.5–9.5 and the elevated temperatures. The activity of laccase@Co3(PO4)2•HNFs declined to 50% of the initial value after 10 reusability cycles, indicating successful immobilization of the enzyme. Structural studies revealed a 32% increase in the α-helix content after hybridization with cobalt phosphate, which improved the activity and stability of the immobilized laccase. Furthermore, the fabricated HNFs exhibited a considerable ability to remove moxifloxacin as an emerging pollutant. The antibiotic (10 mg L−1) was removed by 24% and 75% after 24 h through adsorption and biodegradation, respectively. This study introduces a new method for synthesizing HNFs, which could be used for the fabrication of efficient biocatalysts, biosensors, and adsorbents for industrial, biomedical, and environmental applications.

show abstract

Section: Resultsmentioning

confidence: 98%

Instantaneous synthesis and full characterization of organic–inorganic laccase-cobalt phosphate hybrid nanoflowers

Vojdanitalab

Jafari-Nodoushan

Mojtabavi

et al. 2022

Sci Rep

View full text Add to dashboard Cite

show abstract

“…Moreover, the enzyme molecules are attached to the nanoparticles, and their active sites can be better exposed and are fully in contact with the substrates, thereby improving the catalytic efficiency (Cipolatti et al, 2016). Zheng et al (2018) created organic-inorganic nanoflowers with a Co 2+ -dependent DPE and cobalt phosphate as the organic and inorganic components, respectively. These materials are called nanoflowers because they look like flowers and have many separated nanometer-sized petals.…”

Section: Nanoparticlesmentioning

confidence: 99%

Bioproduction of D‐allulose: Properties, applications, purification, and future perspectives

Jiang

et al. 2021

Comp Rev Food Sci Food Safe

View full text Add to dashboard Cite

D-allulose is the C-3 epimer of D-fructose, which rarely exists in nature, and can be biosynthesized from D-fructose by the catalysis of D-psicose 3-epimerase. Dallulose is safe for human consumption and was recently approved by the United States Food and Drug Administration for food applications. It is not only able be used in food and dietary supplements as a low-calorie sweetener, but also modulates a variety of physiological functions. D-allulose has gained increasing attention owing to its excellent properties. This article presents a review of recent progress on the properties, applications, and bioproduction progress of D-allulose.

show abstract

“…Immobilization technology has dramatically enhanced the stability of enzymes and reduced production costs by improving enzyme reusability. 42 As an immobilized enzyme supporter, Alg(Ti)PDA displayed excellent embedding (100%) and loading rates (113 mg g −1 ). This remarkable characteristic resulted in higher enzyme activity than those of the immobilized enzymes prepared with AlgPDA and Alg.…”

Section: Immobilization For the Fusion Enzymementioning

confidence: 99%

Fusion and secretory expression of an exo‐inulinase and a d‐allulose 3‐epimerase to produce d‐allulose syrup from inulin

et al. 2020

View full text Add to dashboard Cite

BACKGROUND: This study developed a feasible catalytic method for D-allulose syrup production using a fusion enzyme, either in free or immobilized form, through hydrolysis of inulin extracted from Jerusalem artichoke tubers. RESULTS: D-Allulose 3-epimerase (DAE) was actively expressed in secretory form by fusing with the extracellular exo-inulinase CSCA in Escherichia coli BL21 (DE3). The best linker ligating the two enzymes was a flexible peptide containing 12 residues (GSAGSAAGSGEF). At 55°C and pH 8.0, and as with the addition of 1 mmol L −1 Mn 2+ , the CSCA-linkerE-DAE fusion enzyme obtained through high cell-density cultivation displayed a maximal exo-inulinase activity of 21.8 U mg −1 and resulted in a yield of 6.3 g L −1 D-allulose and 39.2 g L −1 D-fructose using 60 g L −1 inulin as the raw material. Catechol-modified alginate with titanium ions (Alg(Ti)PDA) was found to be a promising immobilization material for the fusion enzyme. After conversion for 8 days, the Alg(Ti)PDA-immobilized CSCA-linkerE-DAE (8 U g −1) completed 24 reaction cycles and retained over 80% of its original activity. Each reaction obtained an average of 19.8 g L −1 D-allulose and 32.7 g L −1 D-fructose from 60 g L −1 inulin. CONCLUSION: This study shed light on a feasible and cost-effective approach for the production of syrup containing D-allulose and D-fructose with inulin as the raw material via the use of a CSCA and DAE fusion enzyme. This syrup is of added value as a functional sweetener.

show abstract

Preparation of a Flower-Like Immobilized D-Psicose 3-Epimerase with Enhanced Catalytic Performance

Cited by 39 publications

References 39 publications

Instantaneous synthesis and full characterization of organic–inorganic laccase-cobalt phosphate hybrid nanoflowers

Instantaneous synthesis and full characterization of organic–inorganic laccase-cobalt phosphate hybrid nanoflowers

Bioproduction of D‐allulose: Properties, applications, purification, and future perspectives

Fusion and secretory expression of an exo‐inulinase and a d‐allulose 3‐epimerase to produce d‐allulose syrup from inulin

Contact Info

Product

Resources

About