This product has a minimum activity of 5000 units per gram of liquid. The density of this solution is 1.2 g/mL. The activity is lot specific and reported in the Certificate of Analysis. Please see the link below to review a sample or lot-specific Certificate:
https://www.sigmaaldrich.com/product/sigma/l3170#product-documentation
L3170
Lipase from Candida sp.
recombinant, expressed in Aspergillus niger
Synonym(s):
Lipozyme CALB L
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Product Name
Lipase from Candida sp., recombinant, expressed in Aspergillus niger
recombinant
expressed in Aspergillus niger
form
aqueous solution
enzyme activity
≥5000 LU/g
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
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sustainability
Greener Alternative Product
greener alternative category
storage temp.
2-8°C
Quality Level
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1 of 4
This Item | 54326 | 62288 | 52583 |
|---|---|---|---|
| recombinant expressed in Aspergillus niger | recombinant expressed in Aspergillus oryzae | recombinant expressed in Aspergillus oryzae | recombinant expressed in yeast |
| form aqueous solution | form beads | form powder | form beads |
| storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C | storage temp. 2-8°C |
| Quality Level 200 | Quality Level 100 | Quality Level 100 | Quality Level 100 |
| enzyme activity ≥5000 LU/g | enzyme activity - | enzyme activity - | enzyme activity - |
| greener alternative product characteristics Waste Prevention | greener alternative product characteristics - | greener alternative product characteristics - | greener alternative product characteristics - |
Application
Analysis Note
Minimum 5,000 LU/G of liquid
Biochem/physiol Actions
Lipase from Candida sp or Candida antarctica lipase B (CALB) is enantiospecific for secondary alcohols.[4] It has wide industrial applications.[5] Lipases, in general, catalyze triacylglycerol synthesis and breakdown.[6] Lipase B from Candida antarctica (CALB) undergoes interfacial activation and is a popular lipase.[3]
General description
Lipase from Candida sp or Candida antarctica lipase B (CALB), is a serine hydrolase,[4] which belongs to the α/β hydrolase fold family.[5] It consists of Ser, His, and Asp/Glu catalytic triad and has secondary alcohol binding pocket.[5] Structurally, CALB exists in open and closed conformations[5] and the active site is covered by a small lid.[3] A total of 10 lipases are associated with Candida albicans.[7]
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.
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)
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
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
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Could you please clarify the units or activity (e.g., U/mL) of lipase from Candida sp. (L3420-50 mL), recombinant expressed in Aspergillus oryzae?
1 answer-
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I need to know the percentage of the enzymes in it for calculating its modified activity after a immobilization.I saw another staff in the technical support replied to the same question about item L0777, which was 2%(w/w) lipase. So, can I ask it again?
1 answer-
In addition to the enzyme, this solution contains sodium benzoate, potassium sorbate, Sorbitol, and glycerol. The concentrations are considered proprietary. The density of this preparation is 1.2 g.mL. The activity is lot specific but will be a minimum of 5000 units per gram. Please see the link below to access a sample or lot specific Certificate of Analysis:
https://www.sigmaaldrich.com/product/sigma/l3170#product-documentationHelpful?
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how much enzyme is in it?
1 answer-
This product is sold by units rather than mass weight. The unit value or enzymatic activity is reported on a lot specific basis. The minimum activity specification is 5000 Lipase Units per gram. The unit activity, as well as the density, are reported on the Certificate of Analysis of the lot received. Please see the link below to review a sample Certificate: https://www.sigmaaldrich.com/certificates/COFA/L3/L3170/L3170-BULK________SLCH6228__.pdf
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What is the buffer composition which Product L0777, Lipase is offered in?
1 answer-
The supplier of item considers the buffer composition proprietary.
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