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Key Documents

L3170

Sigma-Aldrich

Lipase from Candida sp.

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recombinant, expressed in Aspergillus niger

Synonyme(s) :

Lipozyme CALB L

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About This Item

Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Produit recombinant

expressed in Aspergillus niger

Niveau de qualité

Forme

aqueous solution

enzyme activity

≥5000 LU/g

Caractéristiques du produit alternatif plus écologique

Waste Prevention
Design for Energy Efficiency
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sustainability

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Autre catégorie plus écologique

Température de stockage

2-8°C

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Description générale

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

Actions biochimiques/physiologiques

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.

Remarque sur l'analyse

Minimum 5,000 LU/G of liquid

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
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
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

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