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Related Concept Videos

Catalytically Perfect Enzymes01:07

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.
Chemical Agents for Microbial Control01:27

Chemical Agents for Microbial Control

Chemicals play important roles in controlling microbial growth by targeting microbial structures and functions as sanitizers, antiseptics, disinfectants, and sterilants.Alcohols are commonly used sanitizers, effectively disrupting lipid membranes, which compromises cell integrity. They are also used as antiseptics and disinfectants due to their rapid action and versatility.Phenols and their derivatives phenolics , known for denaturing proteins and disrupting cell membranes, are particularly...
Enzymes02:34

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...
Microbial Bioremediation of Plastics01:28

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 Enzymes01:22

Introduction to Enzymes

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.’
Most enzymes are proteins that speed up biochemical reactions without being consumed. Enzymes contain one or more active sites that bind the substrates and convert them into products. Many enzymes also...
Restriction Enzymes01:11

Restriction Enzymes

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.
The host bacteria protect their own genomic DNA from these enzymes by methylating these sites. Some...

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Related Experiment Video

Updated: Jun 25, 2026

Isolation and Compositional Analysis of Plant Cuticle Lipid Polyester Monomers
09:47

Isolation and Compositional Analysis of Plant Cuticle Lipid Polyester Monomers

Published on: November 22, 2015

Cutinases: properties and industrial applications.

Tatiana Fontes Pio1, Gabriela Alves Macedo

  • 1Food Science Department, Faculty of Food Engineering, Campinas State University, Campinas, SP, Brazil.

Advances in Applied Microbiology
|February 11, 2009
PubMed
Summary

Cutinases (EC 3.1.1.74) are versatile enzymes with lipase-like activity, stable in various solvents. Their unique properties enable diverse industrial applications, from food processing to polymer chemistry.

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Last Updated: Jun 25, 2026

Isolation and Compositional Analysis of Plant Cuticle Lipid Polyester Monomers
09:47

Isolation and Compositional Analysis of Plant Cuticle Lipid Polyester Monomers

Published on: November 22, 2015

High-throughput Screening of Carbohydrate-degrading Enzymes Using Novel Insoluble Chromogenic Substrate Assay Kits
06:51

High-throughput Screening of Carbohydrate-degrading Enzymes Using Novel Insoluble Chromogenic Substrate Assay Kits

Published on: September 20, 2016

Area of Science:

  • Biochemistry
  • Enzymology
  • Biocatalysis

Background:

  • Cutinases (cutin hydrolases, EC 3.1.1.74) are enzymes from phytopathogenic fungi.
  • They utilize cutin, a plant cuticle biopolymer, as their sole carbon source.
  • Cutin is composed of epoxy and hydroxy fatty acids.

Purpose of the Study:

  • To describe the characteristics of cutinases.
  • To explore their potential industrial applications.
  • To discuss new perspectives for cutinase research and development.

Main Methods:

  • Enzyme discovery from phytopathogenic fungi.
  • Characterization of catalytic properties (hydrolysis, esterification, trans-esterification).
  • Assessment of stability in organic solvents and ionic liquids, including microencapsulation.

Main Results:

  • Cutinases exhibit lipase and esterase-like catalytic activity.
  • They function independently of an oil-water interface.
  • High stability observed in organic solvents and ionic liquids, both free and encapsulated.

Conclusions:

  • Cutinases are valuable biocatalysts due to their unique properties and stability.
  • Potential applications span food, cosmetics, fine chemicals, pesticide degradation, textiles, and polymer chemistry.
  • Further research offers promising avenues for enzyme utilization.