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Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

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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.
 
Most enzymes...
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Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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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...
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Enzymes02:34

Enzymes

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Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
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Cofactors and Coenzymes01:24

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Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
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Introduction to Enzymes01:22

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The use of enzymes by humans dates to 7000 BCE. Humans first used enzymes to ferment sugars and produce alcohol without knowing that this was an enzyme-catalyzed reaction. Wilhelm Kuhne coined the term 'enzyme' in 1877 from the Greek words ‘en’ meaning ‘in’ or ‘within’ and ‘zyme’ meaning ‘yeast.’
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Introduction to Enzyme Kinetics01:19

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Enzyme kinetics studies the rates of biochemical reactions. Scientists monitor the reaction rates for a particular enzymatic reaction at various substrate concentrations. Additional trials with inhibitors or other molecules that affect the reaction rate may also be performed.
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
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Updated: Sep 17, 2025

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
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Sistemas orgánicos covalentes encapsulados con enzimas para la biocatálisis

Satyadip Paul1, Mani Gupta2, Shayan Karak1

  • 1Department of Chemical Sciences, Indian Institute of Science Education and Research, Mohanpur, Kolkata 741246, India.

Journal of the American Chemical Society
|June 27, 2025
PubMed
Resumen

Desarrollamos una síntesis de un solo recipiente para encapsular enzimas en marcos orgánicos covalentes (COF), mejorando su estabilidad y reutilización. Este método mejora el rendimiento de las enzimas en condiciones adversas, lo que permite aplicaciones de biocatálisis más amplias.

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Área de la Ciencia:

  • Biocatálisis
  • Ciencias de los materiales
  • Nanotecnología

Sus antecedentes:

  • Las enzimas son biocatalizadores eficientes, pero presentan una estabilidad limitada en condiciones industriales adversas.
  • El desarrollo de estrategias robustas de inmovilización de enzimas es crucial para expandir sus aplicaciones prácticas.
  • Los marcos orgánicos covalentes (COF) ofrecen una plataforma prometedora para la encapsulación de biomoléculas debido a sus estructuras sintonizables y sus grandes superficies.

Objetivo del estudio:

  • Desarrollar una síntesis acuosa fácil para los COF encapsulados con enzimas.
  • Investigar las interacciones entre las enzimas encapsuladas y la matriz de COF.
  • Evaluar la mayor estabilidad y reutilización de las enzimas encapsuladas.

Principales métodos:

  • Síntesis acuosa de un solo recipiente de TpAzo COF que encapsula varias enzimas, incluidas la beta-glucosidasa (BGL) y la fosfatasa alcalina (ALP).
  • Espectroscopia de correlación de RMN en estado sólido 2D para sondear las interacciones enzima-COF a nivel molecular.
  • Microscopía óptica de barrido de campo cercano tipo dispersión (s-SNOM) y espectroscopia infrarroja con transformación de Fourier a nanoescala (nanoFTIR) para su validación.
  • Ensayos para medir la actividad enzimática, la estabilidad en condiciones de desnaturalización (SDS) y la reciclabilidad.

Principales resultados:

  • Encapsulación exitosa de múltiples enzimas y proteínas dentro del TpAzo COF.
  • Pruebas directas de interacciones moleculares entre las enzimas y la columna vertebral de COF, confirmando la integridad estructural.
  • El BGL y el ALP encapsulados mantuvieron una alta actividad catalítica y fueron reciclables durante hasta diez ciclos.
  • La encapsulación de COF mejoró significativamente la estabilidad de BGL en soluciones SDS del 1 al 15%, mitigando la desnaturalización.

Conclusiones:

  • Se estableció una sólida estrategia de síntesis acuosa de un solo recipiente para compuestos de enzima-COF.
  • Las interacciones enzima-COF son clave para mejorar la estabilidad de la enzima y su reutilización.
  • Este enfoque ofrece un método viable para crear biocatalizadores estables y reutilizables para aplicaciones exigentes.