Immobilized Biocatalysts: Novel Approaches and Tools for Binding Enzymes to Supports

Torres‐Salas, Pamela; Monte-Martínez, Alberto del; Cutiño-Avila, Bessy; Rodríguez-Colinas, Bárbara; Alcalde, Miguel; Ballesteros, Antonio; Plou, Francisco J.

doi:10.1002/adma.201101821

Cited by 158 publications

(117 citation statements)

References 55 publications

(51 reference statements)

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“…However, enzymes (12)(13)(14)(15)(16) are also very important catalytic systems, and recent studies have focused on how to synthesize pure enzymes as well as on how to look for similarities between enzymes and all three catalytic systems on the molecular scale. For example, it is known that, when enzymes are immobilized on a surface, they gain the reusability and ease of separation seen in heterogeneous catalysts, as well as in some cases becoming more stable to wider pH and temperature ranges (61)(62)(63). It is planned to advance previous work by immobilizing enzymes on a solid surface and studying the enzyme-solid interface at the molecular level, and to develop a molecular understanding of all three types of catalysts under similar conditions of reactions and chemical environments.…”

Section: Hybrid Systems: Outlookmentioning

confidence: 99%

Molecular catalysis science: Perspective on unifying the fields of catalysis

Hurlburt

Sabyrov

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Colloidal chemistry is used to control the size, shape, morphology, and composition of metal nanoparticles. Model catalysts as such are applied to catalytic transformations in the three types of catalysts: heterogeneous, homogeneous, and enzymatic. Real-time dynamics of oxidation state, coordination, and bonding of nanoparticle catalysts are put under the microscope using surface techniques such as sumfrequency generation vibrational spectroscopy and ambient pressure X-ray photoelectron spectroscopy under catalytically relevant conditions. It was demonstrated that catalytic behavior and trends are strongly tied to oxidation state, the coordination number and crystallographic orientation of metal sites, and bonding and orientation of surface adsorbates. It was also found that catalytic performance can be tuned by carefully designing and fabricating catalysts from the bottom up. Homogeneous and heterogeneous catalysts, and likely enzymes, behave similarly at the molecular level. Unifying the fields of catalysis is the key to achieving the goal of 100% selectivity in catalysis.Two major breakthroughs have revolutionized molecular catalysis science over the last 20 y. The first is in the development of nanomaterials science (1-4), which has made it possible to synthesize metallic (5-7), bimetallic, and core-shell nanoparticles (8, 9), mesoporous metal oxides (10, 11), and enzymes (12-16) in the nanocatalytic range between 0.8 and 10 nm. The second innovation is in the advancement of spectroscopy and microscopy instruments (17-20)-including nonlinear laser optics (21), sum-frequency generation vibrational spectroscopy (22-24), and synchrotronbased instruments, such as ambient pressure X-ray photoelectron spectroscopy (8,(25)(26)(27), X-ray absorption near-edge structure, extended X-ray absorption fine structure (28-30), infrared (IR) and X-ray microspectroscopies (31), and high-pressure scanning tunneling microscopies (32, 33)-that characterize catalysts at the atomic and molecular levels under reaction conditions (34). Most of the studies that use these techniques focus on nanoscale technologies, such as catalytic energy conversion and information storage, which have reduced the size of transistors to below 25 nm (35).Catalysts are classified into three types-heterogeneous, homogeneous, and enzymatic-and, in most cases, range in size from 1 to 10 nm, which is even smaller than the transistors being developed by the latest size-fabrication technologies. Heterogeneous catalysts work in reaction systems with multiple phases (e.g., solid-gas or solid-liquid phase); homogeneous catalysts reside in the same phase as the reactants, almost always in the liquid phase; and enzymatic catalysts, which are most active in an aqueous solution, make use of active sites in proteins. The catalysis of chemical energy conversion provides ever-increasing selectivity in producing combustible hydrocarbons, gasoline, and diesel.The tenets that direct our catalysis research involve nanoparticle synthesis, characterization under reaction con...

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Section: Hybrid Systems: Outlookmentioning

confidence: 99%

Molecular catalysis science: Perspective on unifying the fields of catalysis

Hurlburt

Sabyrov

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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“…Theoretical Maximum Quantity (tMQ) is defined as the maximum protein quantity to immobilize per g of support (Torres-Salas et al, 2011). In equation 5 MM is the protein molecular mass in Da and mMQ is the molar maximum protein quantity expressed in μmol per g of support.…”

Section: Cystein Protease Assaymentioning

confidence: 99%

“…Ligand Interacting Groups Reactivity (LIGRe) is defined as the proportion between deprotonated (active) and protonated (inactive) ligand surface groups at immobilization pH (Torres-Salas et al, 2011;MonteMartinez and Cutiño-Avila, 2012). Theoretical bases for this calculation are considered on the classical Henderson-Hasselbalch equation (Equation 1) (Henderson, 1908;Hasselbalch, 1917).…”

Section: Cystein Protease Assaymentioning

confidence: 99%

“…New mathematical algorithms and bioinformatics tools (implemented into the program RDID1.0) should be are harmonically combined for designing an optimal immobilization process (Torres-Salas et al, 2011;del Monte-Martínez and Cutiño-Avila, 2012). In this work, RDID1.0 program was employed for the optimization of the covalent immobilization of the cystein proteases bromelain and papain in GlyoxylSepharose CL 4B support for synthesizing optimal affinity chromatography matrix for protease inhibitors purification.…”

Section: Introductionmentioning

confidence: 99%

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Computer-aided design of bromelain and papain covalent immobilization

Cutiño-Avila¹,

Pradas²,

Abreu³

et al. 2014

Rev. Colomb. Biotecnol.

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Enzymes as immobilized derivatives have been widely used in Food, Agrochemical, Pharmaceutical and Biotechnological industries. Protein immobilization is probably the most used technology to improve the operational stability of these molecules. Bromelain (Ananas comosus) and papain (Carica papaya) are cystein proteases extensively used as immobilized biocatalyst with several applications in therapeutics, racemic mixtures resolution, affinity chromatography and others industrial scenarios. The aim of this work was to optimize the covalent immobilization of bromelain and papain via rational design of immobilized derivatives strategy (RDID) and RDID1.0 program. Were determined the maximum protein quantity to immobilize, the optimum immobilization pH (in terms of functional activity retention), was predicted the most probable configuration of the immobilized derivative and the probabilities of multipoint covalent attachment. As support material was used Glyoxyl-Sepharose CL 4B. The accuracy of RDID1.0 program´s prediction was demonstrated comparing with experimental results. Bromelain and papain immobilized derivatives showed desired characteristics for industrial biocatalysis, such as: elevate pH stability retaining 95% and 100% residual activity at pH 7.0 and 8.0, for bromelain and papain, respectively; high thermal stability at 30 °C retaining 90% residual activity for both immobilized enzymes; a catalytic configuration bonded by immobilization at optimal pH; and the ligand load achieve ensure the minimization of diffusional restrictions.Key words: bromelain, covalent immobilization, immobilized derivatives, papain, rational design. ResumenLas enzimas inmovilizadas han sido ampliamente utilizadas en las industrias Alimentaria, Agroquímica, Farmacéutica y Biotecnológica. La inmovilización de proteínas es, probablemente, la tecnología más empleada para elevar la estabilidad operacional de estas moléculas. La bromelina (Ananas comosus) y la papaína (Carica papaya) son cisteín proteasas extensamente usadas como biocatalizadores inmovilizados con disímiles aplicaciones en la terapéutica, resolución de mezclas racémicas, cromatografía de afinidad, entre otros escenarios industriales. El objetivo del presente trabajo fue optimizar la inmovilización covalente de las enzimas bromelina y papaína a través de la estrategia de diseño racional de derivados inmovilizados (RDID) y el programa RDID1.0. Se predijo la cantidad máxima de proteína a inmovilizar, el pH óptimo de inmo- vilización (en términos de retención de la actividad funcional), la configuración más probable del derivado inmovilizado y la probabilidad de enlazamiento covalente multipuntual. Como soporte de inmovilización de empleó Glioxil-Sepharose CL 4B. La precisión de las predicciones llevadas a cabo con el programa RDID1.0 fue validada comparando con los resultados experimentales obtenidos. Los derivados inmovilizados de bromelina y papaína mostraron características deseadas para la biocatálisis a nivel industrial, tales como: elevada estabilidad al pH...

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“…1 Upon immobilization, supported enzymes can provide an easily separable and reusable system (together with enhanced product recovery) which boasts of enhanced resistance to deactivation as compared to free enzymes. 2 Immobilization has several implications when generating increasingly stable biocatalysts compatible with continuous processing technologies. 3 Various strategies to immobilize enzymes on a number of supports have been reported.…”

Section: Introductionmentioning

confidence: 99%

Improving the esterification activity of Pseudomonas fluorescens and Burkholderia cepacia lipases via cross-linked cyclodextrin immobilization

et al. 2014

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The search for a new, efficient and sustainable matrix for biocatalyst immobilization is a growing area in biotechnology. Our proposed approach deals with the utilization of solid cross-linked b-cyclodextrin as supports for enzyme immobilization. Results obtained in terms of enzyme activity and thermal stability of novel immobilised materials have been found to remarkably improve those obtained using commercial immobilized enzymes in esterification reactions (e.g., monostearin synthesis).

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Immobilized Biocatalysts: Novel Approaches and Tools for Binding Enzymes to Supports

Cited by 158 publications

References 55 publications

Molecular catalysis science: Perspective on unifying the fields of catalysis

Molecular catalysis science: Perspective on unifying the fields of catalysis

Computer-aided design of bromelain and papain covalent immobilization

Improving the esterification activity of Pseudomonas fluorescens and Burkholderia cepacia lipases via cross-linked cyclodextrin immobilization

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