Chitosan Co-polymeric nanostructures for catalase immobilization

Inanan, Tülden

doi:10.1016/j.reactfunctpolym.2018.12.013

Cited by 30 publications

(12 citation statements)

References 71 publications

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“…Enzyme immobilization has received a lot of attention since immobilization would provide an enzyme with improved stability, reusability, and control over reactions, as well as lower economic expenses [ 42 ]. As the HMSNs possess a hollow inner cavity and a unique dendritic mesoporous shell, application of the HMSNs as nanoreactors for enzyme-catalyzed reactions was investigated, and the immobilization of catalase was chosen as a proof-of-principle study.…”

Section: Resultsmentioning

confidence: 99%

Dendritic Mesoporous Silica Hollow Spheres for Nano-Bioreactor Application

Zhang

Fang

et al. 2022

Nanomaterials

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Mesoporous silica materials have attracted great research interest for various applications ranging from (bio)catalysis and sensing to drug delivery. It remains challenging to prepare hollow mesoporous silica nanoparticles (HMSN) with large center-radial mesopores that could provide a more efficient transport channel through the cell for guest molecules. Here, we propose a novel strategy for the preparation of HMSN with large dendritic mesopores to achieve higher enzyme loading capacity and more efficient bioreactors. The materials were prepared by combining barium sulfate nanoparticles (BaSO4 NP) as a hard template and the in situ-formed 3-aminophenol/formaldehyde resin as a porogen for directing the dendritic mesopores’ formation. HMSNs with different particle sizes, shell thicknesses, and pore structures have been prepared by choosing BaSO4 NP of various sizes and adjusting the amount of tetraethyl orthosilicate added in synthesis. The obtained HMSN-1.1 possesses a high pore volume (1.07 cm3 g−1), a large average pore size (10.9 nm), and dendritic mesopores that penetrated through the shell. The advantages of HMSNs are also demonstrated for enzyme (catalase) immobilization and subsequent use of catalase-loaded HMSNs as bioreactors for catalyzing the H2O2 degradation reaction. The hollow and dendritic mesoporous shell features of HMSNs provide abundant tunnels for molecular transport and more accessible surfaces for molecular adsorption, showing great promise in developing efficient nanoreactors and drug delivery vehicles.

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Section: Resultsmentioning

confidence: 99%

Dendritic Mesoporous Silica Hollow Spheres for Nano-Bioreactor Application

Zhang

Fang

et al. 2022

Nanomaterials

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“…Data were plotted in triplicate with a standard deviation value of 2.05 (free enzyme) and 1.95 (immobilized enzyme), and the coefficient of variance was less than 1.0 in both cases. Increased K m value of immobilized CAT indicates lower affinity for its substrate H 2 O 2 which is likely to be caused by structural, conformational, or environmental changes of CAT and steric hindrance 10 , 53 , 57 , 58 . But the V max value increased indicating that the activity of the enzyme is retained and is higher even if low concentration of substrate H 2 O 2 is present.…”

Section: Resultsmentioning

confidence: 99%

Purification, characterization, immobilization and kinetic studies of catalase from a novel source Sechium edule

Takio

Yadav

Barman

et al. 2020

Int J of Chemical Kinetics

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A catalase from a novel source Sechium edule (squash) has been purified to homogeneity using ammonium sulfate fractional precipitation, dialysis, and anion exchange chromatography on Diethylaminoethyl (DEAE) cellulose in sodium acetate buffer pH 6.0. The purity of the enzyme was analyzed by SDS-PAGE. The molecular weight of the enzyme using the SDS-PAGE method was found to be 55 kDa with specific activity 6.35 U/mg. The molecular weight of the enzyme was further confirmed by the INTACT mass spectrometric technique and found to be 52.5 kDa. The Reinheitzahl (Rz) value of the enzyme was 1.5. The MALDI-TOF analysis of the purified enzyme showed that it contains 529 amino acid residues. The K m , V max, optimum pH, and optimum temperature of the free enzyme using H 2 O 2 as the substrate were found to be 0.03 mM, 200 μmol/min, 7.6, and 24 • C, respectively. The purified enzyme was immobilized on chitosan beads which was prepared by extracting the chitosan from Cornu aspersum (garden snail) having highest degree of deacetylation%. The kinetic characteristics, K m , V max, optimum pH, and optimum temperature of the immobilized catalase were found to be 0.065 mM, 250 μmol/min, 7.6, and 41 • C, respectively. The immobilized catalase is more thermostable in comparison to free catalase.

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“…The activity of immobilized αamylase is 3-fold higher than that of the free α-amylase at 45 °C. Drastic decrease for the activity of free α-amylase at 45 °C may be explained by structural changes of the enzyme at high temperature values since effect of temperature indicates structural changes [35,36].…”

Section: Effect Of Ph and Temperature On The Activities Of Free And Immobilized Amylasementioning

confidence: 99%

α-Amylase Immobilized Composite Cryogels: Some Studies on Kinetic and Adsorption Factors

Acet

Inanan

Acet

et al. 2021

Appl Biochem Biotechnol

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Stability of enzymes is significant factor for their industrial feasibility. α-amylase is an important enzyme for some industries i.e., textile, food, paper and pharmaceutics.. Pumice particles (PPa) are non-toxic, natural, low-cost alternative adsorbents with high adsorption capacity. In this study, Cu 2+ ions were attached onto pumice particles (Cu 2+ -APPa). Then, Cu 2+ -APPa embedded composite cryogel was synthesized (Cu 2+ -APPaC) via polymerization of gelforming agents at minus temperatures. Characterization studies of the Cu 2+ -APPaC cryogel column was performed by X-ray fluorescence spectrometer (XRF), scanning electron microscopy (SEM), and Brunauer, Emmett, Teller (BET) apparatus. The experiments were carried out in a continuous column system. α-amylase was adsorbed onto Cu 2+ -APPaC cryogel with maximum amount of 858.7 mg/g particles at pH 4.0. Effects of pH and temperature on the activity profiles of the free and the immobilized α-amylase were investigated, and results indicate that immobilization did not alter the optimum pH and temperature values. kcat value of the immobilized α-amylase is higher than that of the free α-amylase while KM value increases by immobilization. Storage and operational stabilities of the free and the immobilized αamylase were determined for 35 days and for 20 runs, respectively.

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Chitosan Co-polymeric nanostructures for catalase immobilization

Cited by 30 publications

References 71 publications

Dendritic Mesoporous Silica Hollow Spheres for Nano-Bioreactor Application

Dendritic Mesoporous Silica Hollow Spheres for Nano-Bioreactor Application

Purification, characterization, immobilization and kinetic studies of catalase from a novel source Sechium edule

α-Amylase Immobilized Composite Cryogels: Some Studies on Kinetic and Adsorption Factors

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