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Related Concept Videos

Carboxylic Acids to Esters: Acid-Catalyzed (Fischer) Esterification Overview01:20

Carboxylic Acids to Esters: Acid-Catalyzed (Fischer) Esterification Overview

The Fischer esterification reaction was developed by the German chemist Emil Fischer in 1895. It is a condensation reaction between carboxylic acids and alcohols in an acidic medium to give esters and water.
Carboxylic Acids to Esters: Acid-Catalyzed (Fischer) Esterification Mechanism01:13

Carboxylic Acids to Esters: Acid-Catalyzed (Fischer) Esterification Mechanism

Carboxylic acids react with alcohols to yield esters via an acid-catalyzed condensation reaction called Fischer esterification. This is a nucleophilic acyl substitution reaction that proceeds via a tetrahedral intermediate, where a water molecule is eliminated as the leaving group.
Esters to Carboxylic Acids: Saponification01:25

Esters to Carboxylic Acids: Saponification

Esters can be hydrolyzed to carboxylic acids under acidic or basic conditions. Base-promoted hydrolysis of esters is a nucleophilic acyl substitution reaction in which esters react with an aqueous base, followed by an acid to give carboxylic acids. This reaction is also known as saponification because it forms the basis for making soaps from fats.
The reaction requires a base in stoichiometric amounts, which participates in the reaction and is not regenerated later. So, the base acts as a...
Esters to Carboxylic Acids: Acid-Catalyzed Hydrolysis01:13

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...
Alkylation of β-Diester Enolates: Malonic Ester Synthesis01:14

Alkylation of β-Diester Enolates: Malonic Ester Synthesis

Malonic ester synthesis is a method to obtain α substituted carboxylic acids from ꞵ-diesters such as diethyl malonate and alkyl halides.
Lipids as Anchors01:32

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...

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Related Experiment Video

Updated: Jul 3, 2026

Preparation, Purification, and Use of Fatty Acid-containing Liposomes
10:43

Preparation, Purification, and Use of Fatty Acid-containing Liposomes

Published on: February 9, 2018

Fatty acid esterification using nylon-immobilized lipase.

A Zaidi1, J L Gainer, G Carta

  • 1Center for Bioprocess Development, Department of Chemical Engineering, University of Virginia, Charlottesville, Virginia 22903-2442.

Biotechnology and Bioengineering
|December 20, 1995
PubMed
Summary
This summary is machine-generated.

This study optimized butyl laurate production using immobilized lipase. Maximum reaction rates were achieved with equimolar substrates and specific temperatures for efficient fatty acid esterification.

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Area of Science:

  • Biocatalysis
  • Enzyme immobilization
  • Organic synthesis

Background:

  • Lipase-catalyzed esterification is crucial for synthesizing fatty acid esters.
  • Enzyme immobilization enhances enzyme stability and reusability in organic media.
  • Candida cylindracea lipase is a viable biocatalyst for esterification reactions.

Purpose of the Study:

  • To investigate the esterification of a long-chain fatty acid using nylon-immobilized lipase.
  • To determine optimal reaction conditions for butyl laurate synthesis.
  • To evaluate the effect of substrate concentration and temperature on reaction rate.

Main Methods:

  • Utilized nylon-immobilized lipase from Candida cylindracea.
  • Conducted esterification in a nearly anhydrous, nonpolar organic medium (hexane).
  • Produced butyl laurate from lauric acid and n-butanol.

Main Results:

  • Achieved a maximum initial reaction rate of 37 mmol/h·g immobilized enzyme.
  • Optimal substrate concentration was 0.5 mol/L in equimolar amounts.
  • Optimal reaction temperature ranged between 35 and 45 degrees C.

Conclusions:

  • Nylon-immobilized Candida cylindracea lipase is effective for butyl laurate synthesis in hexane.
  • Equimolar substrate concentrations and moderate temperatures maximize esterification efficiency.
  • Enzyme immobilization and reaction conditions significantly impact biocatalytic performance.