94129
Immobead 150P
0.15-0.50 mm particle size
Synonym(s):
Copolymer of methacrylate, cross-linked and carrying oxirane groups
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About This Item
Recommended Products
form
beads
loss
≤10% loss on drying
particle size
0.15-0.50 mm
storage temp.
−20°C
Application
Immobead 150 0.15-0.30 mm particle size, a resin for enzyme/protein immobilization, is used for covalent binding of enzymes such as lipases. Bound enzymes are easy to repurify and use in industrial applications.
Storage Class Code
11 - Combustible Solids
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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Colloids and surfaces. B, Biointerfaces, 102, 124-129 (2012-09-27)
Amino-cyclodextrin was covalently attached to multiwalled carbon nanotubes (MWNTs). The functionalized MWNTs have a good dispersibility in water. The lipase was adsorbed onto the functionalized MWNTs. The immobilized lipase was utilized for the resolution of the model compound (R, S)-1-phenyl
Bioresource technology, 115, 141-146 (2012-01-03)
In this work, mixed-mode silica particles functionalized with octyl and sulfonic acid groups was conveniently prepared by co-bonding a mixture of n-octyltriethoxysilane and 3-mercaptopropyltriethoxysilane and then oxidized with hydrogen peroxide. Candida rugosa lipase (CRL) was immobilized on the mixed-mode silica
Langmuir : the ACS journal of surfaces and colloids, 24(23), 13457-13464 (2008-11-11)
A series of epoxy-activated polymer films composed of poly(glycidyl methacrylate/butyl methacrylate/hydroxyethyl methacrylate) were prepared. Variation in comonomer composition allowed exploration of relationships between surface wettability and Candida antartica lipase B (CALB) binding to surfaces. By changing solvents and polymer concentrations
Lipase Immobilization on Hypercrosslinked Polymer Coated Silica for Biocatalytic Synthesis of Phytosterol Esters with Controllable Fatty Acid Composition.
Journal of Agricultural and Food Chemistry (2012)
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