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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
Learn more about the Principles of Green Chemistry.
sustainability
Greener Alternative Product
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
Regulatory Information
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Maísa Pessoa Pinheiro et al.
Biotechnology progress, 34(4), 878-889 (2018-03-15)
Novozyme 435, which is a commercial immobilized lipase B from Candida antarctica (CALB), has been proven to be inadequate for the kinetic resolution of rac-indanyl acetate. As it has been previously described that different immobilization protocols may greatly alter lipase
Minshan Hu et al.
Advances in clinical and experimental medicine : official organ Wroclaw Medical University, 21(6), 751-757 (2013-03-05)
Diet induces changes in plasma lipid profiles, and the plasma lipid profiles vary among different genetic backgrounds. The aim of this study was to investigate how a high-carbohydrate (high-CHO) diet interacts with hepatic lipase G-250A promoter polymorphism to affect the
Effects of bezafibrate treatment in a patient and a carrier with mutations in the PNPLA2 gene, causing neutral lipid storage disease with myopathy.
Tineke van de Weijer et al.
Circulation research, 112(5), e51-e54 (2013-03-02)
Global Trade Item Number
| SKU | GTIN |
|---|---|
| L3170-50ML | 04061833950913 |