Video Experimental Relacionado

Updated: May 8, 2026

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Published on: January 27, 2014

Aprovechar los procesos de auto-reparación y cristalización para la encapsulación eficaz de enzimas en marcos

Yufeng Zhang¹, Chunyan Xing¹, Zhenjie Mu¹

¹Beijing Key Laboratory of Photoelectronic/Electrophotonic Conversion Materials, Key Laboratory of Cluster Science, Ministry of Education, Advanced Technology Research Institute (Jinan), Frontiers Science Center for High Energy Material, Advanced Research Institute of Multidisciplinary Science, School of Chemistry and Chemical Engineering, School of Medical Technology, Beijing Institute of Technology, Beijing 100081, P. R. China.

Journal of the American Chemical Society

|June 7, 2023

Resumen

Una nueva estrategia de prevención inmoviliza eficazmente las enzimas en materiales porosos cristalinos, manteniendo su actividad y estabilidad. Este método supera las limitaciones de tamaño, permitiendo aplicaciones más amplias para los biocatalizadores.

Área de la Ciencia:

Ciencias de los materiales
La bioquímica
Ingeniería Química

Sus antecedentes:

La inmovilización de enzimas en materiales porosos es crucial para las aplicaciones de biocatalizadores.
Los métodos existentes se enfrentan a desafíos como limitaciones en el tamaño de los poros y la desnaturalización de las enzimas debido a las duras condiciones de síntesis.
Los marcos orgánicos covalentes (COF) ofrecen potencial, pero requieren estrategias de encapsulación de enzimas sólidas.

Objetivo del estudio:

Desarrollar una estrategia de preprotección para encapsular enzimas dentro de marcos orgánicos covalentes (COF).
Para superar las limitaciones del tamaño de los poros y las duras condiciones de síntesis en la inmovilización enzimática.
Para crear sistemas de enzimas inmovilizadas robustas y altamente activas.

Principales métodos:

Utilización de la química covalente dinámica de los COF para un proceso de auto-reparación y cristalización.
El uso de una estrategia de preprotección en la que las enzimas se cargan primero en redes de polímeros mesoporosos.
Encapsulación de enzimas durante la cristalización ordenada del polímero en un marco cristalino.

Principales resultados:

Las enzimas se encapsularon con éxito en FOC con una actividad biológica bien mantenida.
Las enzimas COF resultantes mostraron una estabilidad superior en comparación con los métodos convencionales.
La estrategia de preprotección encapsula con éxito enzimas de varios tamaños y cargas superficiales, incluido un sistema de cascada de dos enzimas.

Conclusiones:

La estrategia de preprotección proporciona un enfoque universal para la encapsulación de enzimas en soportes porosos robustos.
Este método evita las limitaciones de tamaño de la enzima y preserva la actividad biocatalítica.
Las enzima@COF desarrolladas son muy prometedoras para aplicaciones de biocatalizadores inmovilizados de alto rendimiento.

Más Videos Relacionados

Microfluidic-based Synthesis of Covalent Organic Frameworks COFs: A Tool for Continuous Production of COF Fibers and Direct Printing on a Surface

Microfluidic-based Synthesis of Covalent Organic Frameworks COFs: A Tool for Continuous Production of COF Fibers and Direct Printing on a Surface

Published on: July 10, 2017

Preparation of Functional Silica Using a Bioinspired Method

Preparation of Functional Silica Using a Bioinspired Method

Published on: August 1, 2018

Videos de Conceptos Relacionados

Autoxidation of Ethers to Peroxides and Hydroperoxides

Autoxidation of Ethers to Peroxides and Hydroperoxides

Ethers represent a class of chemical compounds that become more dangerous with prolonged storage because they tend to form explosive peroxides when standing in the air. Autoxidation is the spontaneous oxidation of a compound in air. In the presence of oxygen, ethers slowly oxidize to form hydroperoxides and dialkyl peroxides.

Catalytically Perfect Enzymes

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.

Introduction to Mechanisms of Enzyme Catalysis

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...

Esters to Carboxylic Acids: Acid-Catalyzed Hydrolysis

Esters to Carboxylic Acids: Acid-Catalyzed Hydrolysis

Hydrolysis of esters under acidic conditions proceeds through a nucleophilic acyl substitution. In the presence of excess water, the reaction proceeds in a reversible manner, forming carboxylic acids and alcohols.
During hydrolysis, the ester is first activated towards nucleophilic attack through the protonation of the carboxyl oxygen atom by the acid catalyst. The protonation makes the ester carbonyl carbon more electrophilic. In the next step, water acts as a nucleophile and adds to the...

Regioselective Formation of Enolates

Regioselective Formation of Enolates

As depicted in the figure below, the unsymmetrical ketones can form two possible enolates: less substituted or more substituted enolates. Usually, the thermodynamic enolates are formed from the more substituted α-carbon atom, while the kinetic enolates are formed faster by deprotonation from the less substituted position. The thermodynamic enolates have lower energy, so they are more stable. But the energy required to form kinetic enolates is less.

Introduction to Mechanisms of Enzyme Catalysis

Introduction to Mechanisms of Enzyme Catalysis

For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes a mild...