Lipase from Burkholderia cepacia

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Cat No.

EXTZ-903

Description

Lipase from Burkholderia cepacia is a triacylglycerol acylhydrolase (EC 3.1.1.3) produced by controlled submerged fermentation and supplied as a white to light yellowish-brown powder with an activity of >= 23,000 units/g. The enzyme catalyzes the hydrolysis of triacylglycerols into glycerol, free fatty acids, and mono- or di-glycerides in aqueous systems, as well as esterification, transesterification, and aminolysis reactions in non-aqueous and low-water media. It remains catalytically active in both water and organic solvents, which makes it one of the most versatile biocatalysts available for chiral synthesis. It is particularly effective in the kinetic resolution of racemic secondary alcohols, carboxylic acids, and esters, and is widely applied in the synthesis of chiral pharmaceutical intermediates, flavor and fragrance compounds, fine chemicals, biodiesel, and structured lipids. The enzyme shows an optimum pH around 8.5, good stability across pH 4.0-11.0, and high catalytic performance at 55-70°C.

Source

Microbial fermentation

Species

Burkholderia cepacia

Applications

Research

Appearance

White to light yellowish-brown powder

Form

Powder

Enzyme Commission Number

EC 3.1.1.3

Activity

>= 23,000 FIP units/g

CAS_No

9001-62-1

Isoelectric point

4.0-11.0

Optimum pH

8.5

Optimum temperature

55-70°C

Thermal stability

Thermally stable up to 55°C

Storage

Store at 2-8°C in a tightly closed container

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Project Description:

For research and industrial use only. Not intended for personal medicinal use. Certain food-grade products are suitable for formulation development in food and related applications.

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