Lipase A
Description
Product Specs
Lipase, classified as EC 3.1.1.3, is an enzyme found widely in nature that breaks down fats and oils. The lipase derived from Serratia marcescens is known for its ability to selectively produce specific mirror-image forms of molecules. It does this particularly well in a process called biocatalytic hydrolysis, where it acts on a compound called trans-3-(4-methoxyphynyl) glycidic acid methyl ester [(±)-MPGM]. This process results in the production of a specific form called (2R, 3S)-3-(4-methoxyphenyl) glycidic acid methyl ester [(-)-MPGM].
Product Science Overview
Lipases are enzymes that catalyze the hydrolysis of fats into glycerol and free fatty acids. They are widely used in various industrial applications, including the production of biodiesel, food processing, pharmaceuticals, and detergents. Recombinant lipases, such as Lipase-A Recombinant, are produced using genetic engineering techniques to enhance their properties and production efficiency.
Recombinant lipases are produced by inserting the gene encoding the lipase enzyme into a suitable host organism. Common hosts for recombinant lipase production include Escherichia coli and Komagataella phaffii (previously known as Pichia pastoris) . These hosts are chosen for their ability to produce high yields of the enzyme and their ease of genetic manipulation.
The production process involves several steps:
- Gene Cloning: The gene encoding the lipase enzyme is isolated and inserted into a plasmid vector.
- Transformation: The plasmid vector is introduced into the host organism, which then expresses the lipase gene.
- Fermentation: The host organism is cultured in a bioreactor under optimal conditions to produce the lipase enzyme.
- Purification: The lipase enzyme is purified from the culture medium using various techniques such as chromatography.
To improve the properties of recombinant lipases, protein engineering techniques such as rational design and directed evolution are employed . These techniques allow scientists to modify the enzyme’s structure to enhance its stability, activity, and specificity.
Additionally, recombinant lipases can be immobilized on various supports to improve their properties and enable their reuse . Immobilization techniques include adsorption, covalent binding, and entrapment. Immobilized lipases are particularly useful in industrial applications where enzyme reuse and stability are critical.
Recombinant lipases have a wide range of applications in various industries :
- Pharmaceuticals: Lipases are used in the synthesis of enantiopure drugs, which are important for producing medications with specific therapeutic effects.
- Food Processing: Lipases are used in the production of flavors, fragrances, and emulsifiers.
- Biodiesel Production: Lipases catalyze the transesterification of triglycerides to produce biodiesel, a renewable and environmentally friendly fuel.
- Detergents: Lipases are used in laundry detergents to break down fats and oils, improving the cleaning efficiency.
