L3170
Lipase from Candida sp.
recombinant, expressed in Aspergillus niger
Synonym(s):
Lipozyme CALB L
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About This Item
Recombinant:
expressed in Aspergillus niger
recombinant
expressed in Aspergillus niger
Quality Level
form
aqueous solution
enzyme activity
≥5000 LU/g
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
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sustainability
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greener alternative category
storage temp.
2-8°C
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
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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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