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Related Concept Videos

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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Enzymes speed up reactions by lowering the activation energy of the reactants. The speed at which the enzyme turns reactants into products is called the rate of reaction. Several factors impact the rate of reaction, including the number of available reactants. Enzyme kinetics is the study of how an enzyme changes the rate of a reaction.
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Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
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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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Restriction Enzymes01:11

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Restriction enzymes are bacterial enzymes used to cut DNA in a sequence-specific manner. To cleave DNA, they bind to specific palindromic sequences called restriction sites. Such palindromic DNA sequences or inverted repeats are commonly found in regions of functional significance, such as the origin of replication, gene operator sites, and regions containing transcription termination signals.
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Standardized Modular Assembly of Polycistronic Operons with Modular Cloning (MoClo) using the In-Cloning toolkit
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A Modular Approach for Interlocking Enzymes in Whatman Paper.

Caterina Riccardi1,2, Shelby McCormick3, Rajeswari Kasi1,2

  • 1Departments of Chemistry, University of Connecticut, Storrs, USA.

Angewandte Chemie (International Ed. in English)
|June 14, 2018
PubMed
Summary

A novel method immobilizes enzymes onto cellulose using bovine serum albumin (BSA) without chemical modification. This approach enhances enzyme stability and activity, offering a versatile solution for enzyme stabilization.

Keywords:
biomaterialsbiosensorscelluloseenzyme stabilitylaccase

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Area of Science:

  • Biotechnology
  • Materials Science
  • Biochemistry

Background:

  • Enzyme immobilization is crucial for industrial applications, but often requires chemical modification of supports, potentially affecting enzyme activity and stability.
  • Cellulose is an abundant, renewable, and biocompatible material, making it an attractive substrate for enzyme immobilization.
  • Existing methods for enzyme attachment to cellulose can be complex and may not universally enhance enzyme performance.

Purpose of the Study:

  • To develop a universal and non-chemical method for enzyme attachment to cellulose.
  • To enhance the stability and retain the high activity of immobilized enzymes.
  • To create a protein-friendly surface on cellulose for enzyme immobilization.

Main Methods:

  • Developed a protein-friendly surface (BSA-Paper) by interlocking bovine serum albumin (BSA) into cellulose without chemical functionalization.
  • Utilized the COOH and NH2 groups on the BSA-Paper surface for subsequent enzyme attachment.
  • Mixed the target enzyme with additional BSA and interlocked them onto the BSA-Paper, forming a second BSA layer that dilutes and crosslinks the enzyme.

Main Results:

  • Laccase immobilized using this method retained over 100% activity and exhibited 240 times greater stability at 25°C (180-day half-life) compared to free laccase.
  • The method demonstrated encouraging results with other enzymes, indicating its potential universality.
  • The non-chemical approach successfully enhanced enzyme stability while preserving high enzymatic activity.

Conclusions:

  • The BSA interlocking method provides a potentially universal approach for enzyme stabilization on cellulose.
  • This technique significantly improves enzyme stability and retains high activity without chemically modifying the cellulose substrate.
  • The developed method offers a robust and efficient strategy for creating highly stable immobilized enzymes for various applications.