62314
Lipase Substrate
for the titrimetric determination of enzyme activity
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grade
for the titrimetric determination of enzyme activity
Quality Level
form
liquid
technique(s)
titration: suitable
refractive index
n20/D 1.36
density
1.05 g/mL at 20 °C
storage temp.
2-8°C
Physical form
aqueous solution with 4.5 mM triolein; 1 M NaCl; 13% (w/v) Triton™ X-100
Other Notes
Assay of microbial lipases with emulsified trioleoyl glycerol; the fatty acids released are titrated with a pH stat
Legal Information
Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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A new assay of microbial lipases with emulsified trioleoyl glycerol.
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Lipases and esterases are responsible for carboxylester hydrolysis inside and outside cells and are useful biocatalysts for (stereo)selective modification of synthetic substrates. Here we describe novel fluorescent suicide inhibitors that differ in structure and polarity for screening and discrimination of
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Analytical biochemistry, 276(1), 72-80 (1999-12-10)
We report on the determination of active enzyme components in pure and crude lipases, using fluorescent inhibitors for covalent modification and visualization of the enzymatically active proteins. Lipase-specific compounds are triacylglycerol analogs, namely 1,2(2, 3)-di-O-alkylglyceroalkylphosphonic acid-p-nitrophenyl esters, containing a fluorescent
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In the postgenomic era new technologies are emerging for global analysis of protein function. The introduction of active site-directed chemical probes for enzymatic activity profiling in complex mixtures, known as activity-based proteomics has greatly accelerated functional annotation of proteins. Here
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