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L3170

Sigma-Aldrich

Lipase from Candida sp.

greener alternative

recombinant, expressed in Aspergillus niger

Synonym(s):

Lipozyme CALB L

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About This Item

Enzyme Commission number:
3.1.1.3 (BRENDA, IUBMB)
MDL number:
MFCD00131509
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in Aspergillus niger

form

aqueous solution

enzyme activity

≥5000 LU/g

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Waste Prevention
Design for Energy Efficiency
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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

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

L3170-50ML:
L3170-BULK:
L3170-VAR:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
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
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
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
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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