Efficient promiscuous Knoevenagel condensation catalyzed by papain confined in Cu 3 (PO 4 ) 2 nanoflowers

et al. 2018

RSC Adv.

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Section: Introductionmentioning

confidence: 99%

Dual-cycle immobilization to reuse both enzyme and support by reblossoming enzyme–inorganic hybrid nanoflowers

et al. 2018

RSC Adv.

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“…The enzyme‐inorganic hybrid nanoflowers were synthesized as previously reported and as in our previous work . 2 mL of CaCl 2 solution (200 mmol L –1 ) was added into 100 mL of a phosphate buffered saline (20 mmol L –1 , pH 6.7) solution containing 0.1 mg mL –1 AKR and 0.033 mg mL –1 ADH.…”

Section: Methodsmentioning

confidence: 99%

“…The enzyme-inorganic hybrid nanoflowers were synthesized as previously reported 18 and as in our previous work. 28 2 mL of CaCl 2 solution (200 mmol L -1 ) was added into 100 mL of a phosphate buffered saline (20 mmol L -1 , pH 6.7) solution containing 0.1 mg mL -1 AKR and 0.033 mg mL -1 ADH. The mixture was then kept still at 4 ∘ C for 24 h. After that, the mixture was centrifuged at 4 ∘ C and 10 000 rpm for 8 min and the supernatant removed.…”

Section: Preparation and Characterization Of Dual-enzyme@cahpo 4 Hybrmentioning

confidence: 99%

Efficient synthesis of the key chiral alcohol intermediate of Crizotinib using dual‐enzyme@CaHPO₄ hybrid nanoflowers assembled by mimetic biomineralization

Chen

J of Chemical Tech & Biotech

et al. 2018

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BACKGROUND To develop an environment‐friendly approach for the synthesis of (S)‐1‐(2,6‐dichloro‐3‐fluorophenyl) ethyl alcohol, an intermediate of anti‐cancer drug Crizotinib, aldehyde ketone reductase and alcohol dehydrogenase were overexpressed in Escherichia coli Rosetta (DE3) and purified via chromatography. Subsequently, they were co‐crystalized with CaHPO4 at 4°C to form dual‐enzyme@CaHPO4 hybrid nanoflowers (hNFs) which was then used to catalyze the synthesis of (S)‐1‐(2,6‐dichloro‐3‐fluorophenyl) ethyl alcohol along with the evaluation of its thermal stability and recycling stability. RESULTS At optimum pH of 7.0, the activities of AKR and ADH confined in the dual‐enzyme@CaHPO4 hybrid nanoflowers were 3.3‐ and 2.1‐fold that of the corresponding free one. The thermos‐stability of confined enzymes was also significantly improved: both enzymes within the hNFs remained more than 80% of initial activities after incubation at 60°C for 8 h, while free enzymes only retained 20% of initial activities under the same treatment conditions. Moreover, AKR and ADH immobilized with a mole ratio of 3:1 confined in hybrid nanoflowers exhibited the highest catalytic activity for the synthesis of chiral ethyl alcohol with a yield up to 90.8% after 12 h. Besides, the final product (S)‐1‐(2,6‐dichloro‐3‐fluorophenyl) ethyl alcohol showed a high ee value of 99.99%. Further, the hybrid nanoflowers retained their initial activity after 16 recycling cycles of synthesis reaction. CONCLUSION The dual‐enzyme@CaHPO4 hybrid nanoflowers efficiently catalyzed synthesis of the chiral compound (S)‐1‐(2,6‐dichloro‐3‐fluorophenyl) ethyl alcohol. The method can also be applied to other multi‐enzyme systems and facilitate their cascade reactions and substrate channeling. © 2018 Society of Chemical Industry

“…It has highly efficient catalytic activity and has higher stability than the free enzyme under severe catalytic conditions. Among the strategies used to obtain the immobilized enzyme preparations, enzyme-inorganic hybrid nanoflowers (hNFs) may be the more conveniently prepared [22] because of the facile procedure and their enhanced activity and stability [22,23], which was inspired from biomineralization and contributes to the green development of chemical enterprises [24]. Currently, the inorganic metal ions used to prepare hNFs have also been expanded from Cu 2+ to Zn 2+ , Co 2+ , Ca 2+ , Mn 2+ , and so forth.…”

Section: Introductionmentioning

confidence: 99%

Facile Bioinspired Preparation of Fluorinase@Fluoridated Hydroxyapatite Nanoflowers for the Biosynthesis of 5′-Fluorodeoxy Adenosine

et al. 2020

Sustainability

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To develop an environmentally friendly biocatalyst for the efficient synthesis of organofluorine compounds, we prepared the enzyme@fluoridated hydroxyapatite nanoflowers (FHAp-NFs) using fluorinase expressed in Escherichia coli Rosetta (DE3) as the biomineralization framework. The obtained fluorinase@FHAp-NFs were characterized by scanning electron microscope (SEM), X-ray diffraction (XRD), and FT-IR spectrum and used in the enzymatic synthesis of 5′-fluorodeoxy adenosin with S-adenosyl-L-methionine and fluoride as substrate. At an optimum pH of 7.5, fluorinase confined in the hybrid nanoflowers presents an approximately 2-fold higher synthetic activity than free fluorinase. Additionally, after heating at 30 °C for 8 h, the FHAp-NFs retained approximately 80.0% of the initial activity. However, free enzyme could remain only 48.2% of its initial activity. The results indicate that the fluoride and hybrid nanoflowers efficiently enhance the catalytic activity and thermal stability of fluorinase in the synthesis of 5′-fluorodeoxy adenosine, which gives a green method for producing the fluorinated organic compounds.