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Enzymes

Enzymes

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.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...

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.

Microbial Bioremediation of Plastics

Microbial Bioremediation of Plastics

Polyethylene terephthalate (PET) is a synthetic polymer widely utilized in the packaging industry, particularly for bottles and containers. Due to its chemical stability and durability, PET accumulates in the environment, contributing significantly to plastic pollution. It comprises repeating units of terephthalic acid and ethylene glycol, resulting in a semi-crystalline structure that is resistant to natural degradation processes.A notable breakthrough in plastic biodegradation came with the...

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...

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...

Enzyme Inhibition

Enzyme Inhibition

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.

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Related Experiment Video

Updated: Jul 2, 2026

Preparation of Functional Silica Using a Bioinspired Method

Preparation of Functional Silica Using a Bioinspired Method

Published on: August 1, 2018

Bioinspired enzyme encapsulation for biocatalysis.

Lorena Betancor¹, Heather R Luckarift

¹Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, UK.

Trends in Biotechnology

|September 2, 2008

Summary

Enzyme immobilization using biomimetic mineralization creates stable, reusable biocatalysts. This method enhances enzyme stability and broadens applications in biocatalysis for novel compound production.

Area of Science:

Biotechnology
Biocatalysis
Materials Science

Background:

Enzyme immobilization is crucial for developing stable and reusable biocatalysts.
Biocatalysis offers a versatile approach for synthesizing novel compounds and natural products.
Enzyme stability and reusability are key challenges in biocatalytic applications.

Purpose of the Study:

To review biomimetic and bioinspired mineral formation as a technique for enzyme immobilization.
To highlight the use of biomimetic mineralization for creating enzyme supports.
To discuss the potential applications of immobilized enzymes in biocatalysis.

Main Methods:

Utilizing biological templates and synthetic analogues for inorganic oxide formation.
Employing biomimetic mineralization to create biocompatible enzyme supports.

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Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability

Published on: April 22, 2016

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Published on: January 27, 2014

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Last Updated: Jul 2, 2026

Preparation of Functional Silica Using a Bioinspired Method

Preparation of Functional Silica Using a Bioinspired Method

Published on: August 1, 2018

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability

Published on: April 22, 2016

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Synthesis of an Intein-mediated Artificial Protein Hydrogel

Published on: January 27, 2014

Entraining and attaching encapsulated enzymes to various support materials.

Main Results:

Biomimetic mineralization provides excellent supports for enzyme stabilization.
Inorganic oxide materials generated offer biocompatible environments for enzymes.
The method allows for effective enzyme encapsulation and attachment to supports.

Conclusions:

Biomimetic mineralization is a versatile technique for enzyme immobilization.
This approach enhances enzyme stability, leading to robust biocatalysts.
Immobilized enzymes via this method have broad potential in biocatalytic processes.