Facile immobilization of enzyme on three dimensionally ordered macroporous silica via a biomimetic coating

Jiang, Yanjun; Wang, Yaping; Wang, Hua; Zhou, Liya; Gao, Jing; Zhang, Yufei; Zhang, Xu; Wang, Xiaomei; Li, Jian

doi:10.1039/c4nj01947d

Cited by 32 publications

(18 citation statements)

References 34 publications

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“…The polydopamine on the surface of DPMS contains quinones, which are reactive toward nucleophilic groups and can react with the amino or thiol groups of the lipase, and this reaction can lead to the immobilization of lipase in DPMS via covalent bond formation between the polydopamine and the lipase molecules1625. The more acidic optimal pH of LCS@DPMS might be caused by the following two reasons: (i) the covalent attachment between the lipase and polydopamine on the surface of the support that limited the transition of lipase conformation against the change of pH1226, and (ii) the amine or imines groups on the surface of polydopamine near the active sites of lipase molecules could diminish the concentration of protons1517. Additionally, the pH profile of LCS@DPMS was wider range than free lipase and LCS@MS, which enhanced stability of LCS@DPMS under acidic conditions.…”

Section: Resultsmentioning

confidence: 99%

“…Typical strategies for immobilizing enzymes onto mesoporous silicas rely on surface grafting via polymers containing functional groups or low molecular weight linkers to which enzymes are reacted by covalent conjugation101112. But such immobilization methods are usually accompanied by enzymes deactivation13.…”

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confidence: 99%

“…Furthermore, the dopamine molecules contain both catechol and primary amine, which are capable of immobilizing biomolecules1516. Therefore, immobilizing enzymes onto different substrates modified with dopamine can be easily achieved by facile conjugation of proteins12151617. However, to the best of our knowledge, Meso-Onion-S modified with dopamine has never been used as enzyme immobilization support.…”

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confidence: 99%

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Dopamine-functionalized mesoporous onion-like silica as a new matrix for immobilization of lipase Candida sp. 99-125

Gao

Jiang

et al. 2017

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Dopmine functionalized mesoporous onion-like silica (DPMS) was synthesized via a biomimetic coating, and lipase Candida sp. 99-125 (LCS) was immobilized in DPMS (LCS@DPMS) by physical adsorption in this study. The DPMS was characterized by SEM, TEM, BET and FT-IR, and it was shown that the DPMS had clear multishell structures with large surface area of 419 m2/g. The activity, pH stability, thermal stability, storage stability, and reusability of the LCS@DPMS were investigated in detail. The stabilities of LCS@DPMS were improved significantly compared to the free lipase and LCS@MS (LCS immobilized in unfunctionalized mesoporous onion-like silica by physical adsorption). All the results indicated that the DPMS had high efficiency and improved stability for lipase immobilization.

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Dopamine-functionalized mesoporous onion-like silica as a new matrix for immobilization of lipase Candida sp. 99-125

Gao

Jiang

et al. 2017

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“…43 One unit of enzymatic activity defined as the PGA amount required to produce 1 mmol of 6-APA per min. 43 One unit of enzymatic activity defined as the PGA amount required to produce 1 mmol of 6-APA per min.…”

Section: Assay Of Free and Immobilized Pgamentioning

confidence: 99%

MOF-templated rough, ultrathin inorganic microcapsules for enzyme immobilization

et al. 2015

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Ultrathin titania microcapsules with rough surfaces were prepared by using a metal-organic framework (ZIF-8) as one kind of hard template to mediate the structures of the microcapsule shell. Specifically, CaCO 3 particles were first coated with tannic acid (TA) followed by the deposition of hydrophobic ZIF-8 and another TA layer, the obtained particles were then assembled with protamine/TiO 2 bilayers through biomimetic mineralization. Finally, the microcapsules (Z-TiO 2 ) were obtained after simultaneously removing CaCO 3 and ZIF-8 templates using ethylenediaminetetraacetic acid (EDTA). The coordination interaction between TA and ZIF-8 ensured the robust templating which endowed the microcapsules with a rough surface and an ultrathin microcapsules shell (100 nm) with 4.4 nm pore size. Moreover, the surface roughness of microcapsules can be regulated by changing the size of ZIF-8 crystals. The microcapsules were then utilized to immobilize penicillin G acylase (PGA). And PGA@Z-TiO 2 retained 69% activity of equivalent free PGA with a loading capacity of 160 mg g À1 . The PGA@Z-TiO 2 microcapsules exhibited superior reusability: after recycling 8 times, the conversion of the enzymatic reaction remained 36.0%, which was twice higher than that of PGA@TiO 2 (14.7%). Moreover, compared with free PGA and PGA@TiO 2 microcapsules, PGA@Z-TiO 2 microcapsules exhibited higher thermal and storage stability. After storing for 60 days, the relative activity of PGA@Z-TiO 2 remained 89.6%, which was higher than that of free PGA (34.5%) and PGA@TiO 2 (73.6%). ZIF-8 can be envisioned to be a novel class of hard template for preparing a broad variety of microcapsules with different hierarchical structures. † Electronic supplementary information (ESI) available: SEM and TEM images of ZIF-8 particles, nitrogen adsorption-desorption isotherms of ZIF-8 particles, and UV-vis spectra of the assembled multilayer film. See Fig. 12 Recycling stability of PGA@Z-TiO 2 and PGA@TiO 2 (a), temperature stability (b), pH stability (c), and storage stability (d) of free PGA, PGA@Z-TiO 2 and PGA@TiO 2 MCs.

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“…Immobilization of enzymes is an essential facet of modern biotechnology. Enzyme immobilization (especially on magnetic carriers) offers many advantages when compared with soluble enzyme preparations, including the ability to improve the catalytic properties of the enzyme, easy enzyme recovery and reuse, and reduced catalytic processing costs [18][19][20]. Various methods, including physical adsorption, covalent binding, cross-linking, entrapment and encapsulation, have been used for enzyme immobilization.…”

Section: Introductionmentioning

confidence: 99%

Highly Efficient Synthesis of 2,5-Dihydroxypyridine using Pseudomonas sp. ZZ-5 Nicotine Hydroxylase Immobilized on Immobead 150

et al. 2018

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In this report, the use of immobilized nicotine hydroxylase from Pseudomonas sp. ZZ-5 (HSPHZZ) for the production of 2,5-dihydroxypyridine (2,5-DHP) from 6-hydroxy-3-succinoylpyridine (HSP) in the presence of nicotinamide adenine dinucleotide (NADH) and flavin adenine dinucleotide (FAD) is described. HSPHZZ was covalently immobilized on Immobead 150 (ImmHSPHZZ). ImmHSPHZZ (obtained with 5–30 mg of protein per gram of support) catalyzed the hydrolysis of HSP to 2,5-DHP. At a protein loading of 15 mg g−1, ImmHSPHZZ converted 93.6% of HSP to 2,5-DHP in 6 h. The activity of ImmHSPHZZ was compared with that of free HSPHZZ under various conditions, including pH, temperature, enzyme concentration, substrate concentration and stability over time, and kinetic parameters were measured. The results showed that ImmHSPHZZ performed better over wider ranges of pH and temperature when compared with that of HSPHZZ. The optimal concentrations of ImmHSPHZZ and substrate were 30 mg L−1 and 0.75 mM, respectively. Under optimal conditions, 94.5 mg L−1 of 2,5-DHP was produced after 30 min with 85.4% conversion. After 8 reaction cycles and 6 days of storage, 51.3% and 75.0% of the initial enzyme activity remained, respectively. The results provide a framework for development of commercially suitable immobilized enzymes that produce 2,5-DHP.

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Facile immobilization of enzyme on three dimensionally ordered macroporous silica via a biomimetic coating

Cited by 32 publications

References 34 publications

Dopamine-functionalized mesoporous onion-like silica as a new matrix for immobilization of lipase Candida sp. 99-125

Dopamine-functionalized mesoporous onion-like silica as a new matrix for immobilization of lipase Candida sp. 99-125

MOF-templated rough, ultrathin inorganic microcapsules for enzyme immobilization

Highly Efficient Synthesis of 2,5-Dihydroxypyridine using Pseudomonas sp. ZZ-5 Nicotine Hydroxylase Immobilized on Immobead 150

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