54327
Lipase, immobilized on Immobead 150 from Pseudomonas cepacia
≥900 U/g
Synonym(s):
Immobilized Lipase
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About This Item
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
biological source
bacterial (Pseudomonas cepacia)
Quality Level
form
powder (or beads)
specific activity
≥900 U/g
color
white to off-white
application(s)
life science and biopharma
storage temp.
2-8°C
Gene Information
Burkholderia spp. ... BURCE16_RS29975(56665765)
Related Categories
Application
Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.
Biochem/physiol Actions
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_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificates of Analysis (COA)
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ACS omega, 6(43), 29192-29200 (2021-11-09)
Deracemizations are clearly preferable to kinetic resolutions in the production of chiral molecules from racemates, as they allow up to 100% chemical and optical yield. Here we present a new process route for multienzymatic deracemizations that is relevant for reaction
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Protein fatty acylation regulates numerous cell signaling pathways. Polyunsaturated fatty acids (PUFAs) exert a plethora of physiological effects, including cell signaling regulation, with underlying mechanisms to be fully understood. Herein, we report that docosahexaenoic acid (DHA) and eicosapentaenoic acid (EPA)
Guan-Chun Chen et al.
Biotechnology letters, 33(3), 525-529 (2010-11-04)
Triacylglycerol lipase from Pseudomonas cepacia and Fe(3)O(4) magnetic nanoparticles were encapsulated simultaneously within biomimetic silica through the catalysis of polyallylamine. The encapsulation efficiency reached 96% with an activity recovery of 51%. After 5 h at 37°C, the activities of the
Industrial applications of microbial lipases
F. Hasan et al.
Enzyme and Microbial Technology, 39, 235-251 (2006)
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