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About This Item
NACRES:
NA.54
UNSPSC Code:
12352204
Product Name
Lipase B Candida antarctica immobilized on Immobead 150, recombinant from Aspergillus oryzae, ≥1800 U/g
biological source
fungus (Candida antarctica)
recombinant
expressed in Aspergillus oryzae
form
beads
specific activity
≥1800 U/g
technique(s)
analytical sample preparation: suitable
color
white to off-white
application(s)
life science and biopharma
storage temp.
2-8°C
Quality Level
Gene Information
fungus ... LIPB(1170790)
Application
Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.
Biochem/physiol Actions
Lipase B from Candida antarctica (CAL-B) acts as a catalyst for producing amines, amides, and alcohols.. It is used as a biocatalyst in research and industry. CAL-B is involved in the hydrolysis of triglycerides. Lipases catalyze the hydrolysis of triacylglycerols into glycerol and free fatty acids.
General description
Research area: Cell Signaling
Lipase B from Candida antarctica (CAL-B) is a serine hydrolase, α/β-hydrolase, and is a member of the lipase family. CAL-B is composed of an α/β-hydrolase fold and the active site contains a Ser-His-Asp catalytic triad.
Lipase B from Candida antarctica (CAL-B) is a serine hydrolase, α/β-hydrolase, and is a member of the lipase family. CAL-B is composed of an α/β-hydrolase fold and the active site contains a Ser-His-Asp catalytic triad.
Other Notes
1 U corresponds to the amount of enzyme which liberates 1 μmol butyric acid per minute at pH 7.5 and 40°C (tributyrin, Cat. No. 91010, as substrate)
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
常规特殊物品
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Biotechnological relevance of the lipase A from Candida antarctica
Monteiro RRC, et al.
Catalysis Today, 362, 141-154 (2021)
Interfacial activation of Candida antarctica lipase B: combined evidence from experiment and simulation
Themistoklis Z, et al.
Biochemistry, 54(38), 5969?5979- 5969?5979 (2015)
Karel Pomeisl et al.
Bioorganic & medicinal chemistry, 27(7), 1246-1253 (2019-02-20)
An enzymatic alternative to the chemical synthesis of chiral gem-difluorinated alcohols has been developed. The method is highly effective and stereoselective, feasible at laboratory temperature, avoiding the use of toxic heavy metal catalysts which is an important benefit in medicinal
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