L3170

Sigma-Aldrich

Lipase from Candida sp.

greener alternative

recombinant, expressed in Aspergillus niger

Synonym(s):
Lipozyme CALB L
Enzyme Commission number:
MDL number:
NACRES:
NA.54

Quality Level

recombinant

expressed in Aspergillus niger

form

aqueous solution

enzyme activity

≥5000 LU/g

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

greener alternative category

Enabling

storage temp.

2-8°C

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General description

Lipase from Candida sp or Candida antarctica lipase B (CALB), is a serine hydrolase, which belongs to the α/β hydrolase fold family. It consists of Ser, His, and Asp/Glu catalytic triad and has secondary alcohol binding pocket. Structurally, CALB exists in open and closed conformations and the active site is covered by a small lid. A total of 10 lipases are associated with Candida albicans.
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in biodiesel research. For more information see the article in biofiles.

Application

Lipase from Candida sp. has been used:
  • in Gold nanoparticles (AuNPs) conjugate preparation for biophysical studies
  • in lipase activity assay
  • for immobilization with Immobead-350

Biochem/physiol Actions

Lipase from Candida sp or Candida antarctica lipase B (CALB) is enantiospecific for secondary alcohols. It has wide industrial applications. Lipases, in general, catalyze triacylglycerol synthesis and breakdown. Lipase B from Candida antarctica (CALB) undergoes interfacial activation and is a popular lipase.

Analysis Note

Minimum 5,000 LU/G of liquid

RIDADR

NONH for all modes of transport

WGK Germany

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis
Certificate of Origin
Dongming Lan et al.
International journal of molecular sciences, 12(10), 7216-7237 (2011-11-11)
Lipases from microorganisms have multi-faceted properties and play an important role in ever-growing modern biotechnology and, consequently, it is of great significance to develop new ones. In the present work, a lipase gene from Candida albicans (CaLIP10) was cloned and...
Benjamin Stauch et al.
Journal of lipid research, 56(12), 2348-2358 (2015-10-09)
Lipases (EC 3.1.1.3) are ubiquitous hydrolases for the carboxyl ester bond of water-insoluble substrates, such as triacylglycerols, phospholipids, and other insoluble substrates, acting in aqueous as well as in low-water media, thus being of considerable physiological significance with high interest...
Physicochemical Study of the Interaction between Gold Nanoparticles and Lipase from Candida sp.(CALB): Insights into the Nano-Bio Interface
Barros HR de, et al.
Journal of the Brazilian Chemical Society, 30(10), 2231-2242 (2019)
Christoph Buerth et al.
Applied microbiology and biotechnology, 98(11), 4963-4973 (2014-01-29)
CalB of Pseudozyma aphidis (formerly named Candida antarctica) is one of the most widely applied enzymes in industrial biocatalysis. Here, we describe a protein with 66 % sequence identity to CalB, designated Ustilago maydis lipase 2 (Uml2), which was identified as...
Attila Gácser et al.
Infection and immunity, 75(10), 4710-4718 (2007-07-25)
The production of lipases can affect microbial fitness and virulence. We examined the role of the lipase 8 (LIP8) gene in the virulence of Candida albicans by constructing Deltalip8 strains by the URA-blaster disruption method. Reverse transcription-PCR experiments demonstrated the...

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