54326
Lipase B Candida antarctica immobilized on Immobead 150, recombinant from Aspergillus oryzae
≥1800 U/g
Synonym(s):
Candida lipase, Immobilized lipase, Recombinant lipase
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About This Item
UNSPSC Code:
12352204
NACRES:
NA.54
biological source
fungus (Candida antarctica)
Quality Level
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
Gene Information
fungus ... LIPB(1170790)
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.
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.
Unit Definition
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)
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Certificates of Analysis (COA)
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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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