Catalytic properties of maltogenic α-amylase from Bacillus stearothermophilus immobilized onto poly(urethane urea) microparticles

Strakšys, Antanas; Kochanė, Tatjana; Budrienė, Saulutė

doi:10.1016/j.foodchem.2016.05.071

Cited by 25 publications

(14 citation statements)

References 17 publications

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“…However, such interactions are unstable under the conditions of the desorption tests. In fact, the immobilized enzyme retained its catalytic properties, which indicates that covalent bonds are also present between the biomolecules and support material [29]. This is confirmed by the findings of Hirsh et al, who used polystyrene film after surface activation by plasma immersion ion implantation.…”

Section: Cellulase Immobilizationsupporting

confidence: 67%

Immobilization of Cellulase on a Functional Inorganic–Organic Hybrid Support: Stability and Kinetic Study

et al. 2017

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Abstract:Cellulase from Aspergillus niger was immobilized on a synthesized TiO 2 -lignin hybrid support. The enzyme was effectively deposited on the inorganic-organic hybrid matrix, mainly via physical interactions. The optimal initial immobilization parameters, selected for the highest relative activity, were pH 5.0, 6 h process duration, and an enzyme solution concentration of 5 mg/mL. Moreover, the effects of pH, temperature, and number of consecutive catalytic cycles and the storage stability of free and immobilized cellulase were evaluated and compared. Thermal and chemical stability were significantly improved, while after 3 h at a temperature of 50 • C and pH 6.0, the immobilized cellulase retained over 80% of its initial activity. In addition, the half-life of the immobilized cellulase (307 min) was five times that of the free enzyme (63 min). After ten repeated catalytic cycles, the immobilized biocatalyst retained over 90% of its initial catalytic properties. This study presents a protocol for the production of highly stable and reusable biocatalytic systems for practical application in the hydrolysis of cellulose.

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Section: Cellulase Immobilizationsupporting

confidence: 67%

Immobilization of Cellulase on a Functional Inorganic–Organic Hybrid Support: Stability and Kinetic Study

et al. 2017

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“…beads mainly by relatively stable covalent bonds. This finding is in consistence with what is suggested for other carriers [32]. [1,33].…”

Section: Effect Of Salt and Ca 2+ Ionssupporting

confidence: 92%

Textural and Structural Characterizations of Mesoporous Chitosan Beads for Immobilization of Alpha-Amylase: Diffusivity and Sustainability of Biocatalyst

Darzi

Gilani

Farrokhi

et al. 2019

IJE

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In the present study, textural and structural characterizations of chitosan bead for immobilization of alpha amylase in detail by N2 adsorption-desorption, Microspore Analysis (MP), Barrett-Joyner-Halenda (BJH) plots and Field Emission Scanning Electron Microscope (FESEM) observations were investigated. Pore structure observation revealed chemical activation of chitosan bead by glutaraldehyde can change both the isotherm type of adsorption and pores shape. In consistence with textural analysis, the high value of pore volume distribution with range of mesopores region indicated the porosity of activated chitosan bead was uniformly increased. Intra-particle diffusion model designated that 97.6% of amylase was adsorbed inside the mesopores of activated chitosan bead owing to increase in kid (rate constant) and reduce of boundary layer effect on diffusion process. In addition, the stability experiments (pH, storage and thermal stability), enzyme leakage, Ca 2+ and salt concentration effects were evaluated for immobilized amylase and compared with its free activities. Ca 2+ concentration of 1 mM shows an excellent impact on relative activity of amylase on its free and immobilized forms. NaCl experiments indicated that 84% of amylase was covalently immobilized on activated chitosan beads. Further, the Michaelis-Menten kinetic coefficients, Km (~0.4mg/ml) and, Vmax(~227 U/mg Enzyme), point out strong affinity and high activity of immobilized enzym.

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“…In this work HMDI was used for PU synthesis. Obtained efficiency of immobilization onto those PU microparticles was higher than obtained previously, when isophorone diisocyanate was used for synthesis of PU [54]. However the main disadvantage of this method is relatively fast inactivation of PU carrier reactive groups which are needed for covalent enzyme immobilization.…”

Section: Enzyme Immobilizationmentioning

confidence: 75%

“…Amount of isocyanate groups determined imediately after synthesis of PU microparticles was 4.5 %. Poly(vinyl alcohol) (PVA) based PU microparticles are more "environmental friendly" due to biodegradable and biocompatible PVA used for the synthesis instead of common diols, such as butanediol, hexanediol, etc [52,54,55].…”

Section: Au-nps Hydrodynamic Diameter Distribution Histograms Obtainementioning

confidence: 99%

Polyurethane-gold and polyurethane-silver nanoparticles conjugates for efficient immobilization of maltogenase

Kochanė

Budrienė

Miasojedovas

et al. 2017

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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Catalytic properties of maltogenic α-amylase from Bacillus stearothermophilus immobilized onto poly(urethane urea) microparticles

Cited by 25 publications

References 17 publications

Immobilization of Cellulase on a Functional Inorganic–Organic Hybrid Support: Stability and Kinetic Study

Immobilization of Cellulase on a Functional Inorganic–Organic Hybrid Support: Stability and Kinetic Study

Textural and Structural Characterizations of Mesoporous Chitosan Beads for Immobilization of Alpha-Amylase: Diffusivity and Sustainability of Biocatalyst

Polyurethane-gold and polyurethane-silver nanoparticles conjugates for efficient immobilization of maltogenase

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