L3170
Lipase from Candida sp.
recombinant, expressed in Aspergillus niger
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Synonym(s):
Lipozyme CALB L
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
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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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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.
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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
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Customers Also Viewed
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
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
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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