Enzyme distribution and matrix characteristics in biocatalytic particles

Roon, J.L. van; Boom, R.M.; Paasman, M. A.; Tramper, J.; Schroën, C.G.P.H.; Beeftink, H.H.

doi:10.1016/j.jbiotec.2005.04.012

Cited by 6 publications

(4 citation statements)

References 18 publications

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“…3a. Table 1 summarizes the analytical methods for measurement of the distribution of bound proteins on surfaces and more specifically inside porous supports [22,[31][32][33][34][35][36][51][52][53][54][55][56][57][58]. Level of application, strengths and limitations are pointed out.…”

Section: Enzyme Loading In High Capacity and High Quality For Immobilmentioning

confidence: 99%

Advanced characterization of immobilized enzymes as heterogeneous biocatalysts

2016

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Section: Enzyme Loading In High Capacity and High Quality For Immobilmentioning

confidence: 99%

Advanced characterization of immobilized enzymes as heterogeneous biocatalysts

2016

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“…Microscopy data has been proved a valuable method for determining the distribution of the enzymes in or on the solid material and has thus facilitated interpreting the characteristics of the immobilized enzymes . These methods include light microscopy, confocal laser scanning microscopy (CLSM), cryotemperature field-emission scanning electron microscopy (cryo-FESEM), and spherical aberration (Cs)-corrected scanning TEM. , Spectroscopy and scattering experiments have also been employed, including Raman spectroscopy and small angle X-ray scattering (SAXS). CLSM in combination with fluorescent protein labeling has been widely applied to MOF biocomposites.…”

Section: Characterization Of Mof Immobilized Enzymesmentioning

confidence: 99%

Metal–Organic Framework-Based Enzyme Biocomposites

et al. 2021

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Due to their efficiency, selectivity, and environmental sustainability, there are significant opportunities for enzymes in chemical synthesis and biotechnology. However, as the three-dimensional active structure of enzymes is predominantly maintained by weaker non-covalent interactions, thermal, pH and chemical stressors can modify or eliminate activity. Metal-organic Frameworks (MOFs), which are extended porous network materials assembled by a bottom-up building block approach from metal-based nodes and organic linkers, can be used to afford protection to enzymes. The self-assembled structures of MOFs can be used to encase an enzyme in a process called encapsulation when the MOF is synthesized in the presence of the biomolecule. Alternatively, enzymes can be infiltrated into mesoporous MOF structures or surface bound via covalent or non-covalent processes. Integration of MOF materials and enzymes in this way affords protection and allows the enzyme to maintain activity in challenge conditions (e.g. denaturing agents, elevated temperature, non-native pH and organic solvents). In addition to forming simple enzyme/MOF biocomposites, other materials can be introduced to the composites to improve recovery or facilitate advanced applications in sensing and fuel cell technology. This review canvasses enzyme protection via encapsulation, pore infiltration and surface adsorption and summarizes strategies to form multi-component composites. Also, given that enzyme/MOF biocomposites straddle materials chemistry and enzymology, this review provides an assessment of the characterization methodologies used for MOF-immobilized enzymes and identifies some key parameters to facilitate development of the field. CONTENTSMOF-based enzyme biocomposite compositions and the concept of encapsulation 3.MOF-based enzyme biocomposites formed via encapsulation 3.1.Templating methods 3.2.One-pot embedding (non-templated) 3.3.Parameters influencing the chemistry of enzyme@MOF biocomposites 3.3.1. Additives 3.3.2.Enzyme suface chemistry 3.3.3.MOF precusors and structures 3.4.Alternative synthesis strategies 4.Infiltration (post insertion of enzymes in preformed MOFs) 4.1.Early results and the advantages of MOFs for infiltration 4.2.Tuning the framework structure in infiltrated enzyme@MOF biocomposites 4.3.Towards applications of infiltrated enzyme@MOFs 5.Surface bound enzymes 5.1. Immobilization via physical adsorption 5.2. Immobilization via coordinate bonds 5.3. Immobilization via covalent bonding 5.4. Enzymatic activity upon surface-immobilization 6. Multicomponent biocomposites 7. Characterization of MOF immobilized enzymes 7.1. Overview 7.2. Key immobilization parameters 7.3. One-pot enzyme MOF formation 7.4. Highlights of MOF-immobilized enzyme performance 7.4.1. Experimental determination of key immobilization parameters 7.4.1.1. Determination of protein concentrations 7.4.1.2. Activity determination 7.4.2. Advanced characterization of immobilized enzymes 7.4.2.1. Apparent enzyme kinetics 7.4.2.2. Structural analysis and localization o...

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“…It was shown previously that Assemblase particles are polydisperse (Van Roon et al 2003) and, to some extent, polymorph (Van Roon et al 2005b). A formal treatment of mass transfer processes in such particles would involve an exact three-dimensional analysis of each particle and its contribution to the total volume (or mass) of biocatalytic particles, which is extremely laborious.…”

Section: Geometry and Particle Sizementioning

confidence: 99%

“…A formal treatment of mass transfer processes in such particles would involve an exact three-dimensional analysis of each particle and its contribution to the total volume (or mass) of biocatalytic particles, which is extremely laborious. Instead, spherical particle geometry was assumed; scanning electron microscopic (Van Roon et al 2005b) micrographs of supercritically dried Assemblase particles indicate that this assumption is not too far off. From the particle size distribution (Van Roon et al 2003), a characteristic particle was defined as the particle at the 50% point of the cumulative volume distribution (205-μm radius).…”

Section: Geometry and Particle Sizementioning

confidence: 99%

A multicomponent reaction–diffusion model of a heterogeneously distributed immobilized enzyme

Roon

Arntz

Kallenberg

et al. 2006

Appl Microbiol Biotechnol

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A physical model was derived for the synthesis of the antibiotic cephalexin with an industrial immobilized penicillin G acylase, called Assemblase. In reactions catalyzed by Assemblase, less product and more by-product are formed in comparison with a free-enzyme catalyzed reaction. The model incorporates reaction with a heterogeneous enzyme distribution, electrostatically coupled transport, and pH-dependent dissociation behavior of reactants and is used to obtain insight in the complex interplay between these individual processes leading to the suboptimal conversion. The model was successfully validated with synthesis experiments for conditions ranging from heavily diffusion limited to hardly diffusion limited, including substrate concentrations from 50 to 600 mM, temperatures between 273 and 303 K, and pH values between 6 and 9. During the conversion of the substrates into cephalexin, severe pH gradients inside the biocatalytic particle, which were previously measured by others, were predicted. Physical insight in such intraparticle process dynamics may give important clues for future biocatalyst design. The modular construction of the model may also facilitate its use for other bioconversions with other biocatalysts.

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Enzyme distribution and matrix characteristics in biocatalytic particles

Cited by 6 publications

References 18 publications

Advanced characterization of immobilized enzymes as heterogeneous biocatalysts

Advanced characterization of immobilized enzymes as heterogeneous biocatalysts

Metal–Organic Framework-Based Enzyme Biocomposites

A multicomponent reaction–diffusion model of a heterogeneously distributed immobilized enzyme

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