A lipoprotein lipase (LPL) was made water insoluble by immobilizing onto the surface of polyacrolein (PAA) microspheres with and without oligoglycines a s spacer. The activity of the immobilized LPL was found to remain high toward a small ester substrate, p-nitrophenyl laurate (pNPL). The relative a
Lipoprotein lipase immobilization onto porous polyvinyl alcohol beads
β Scribed by Toshio Hayashi; Soung-Hyu Hyon; Won-Ill Cha; Yoshito Ikada
- Publisher
- John Wiley and Sons
- Year
- 1993
- Tongue
- English
- Weight
- 586 KB
- Volume
- 49
- Category
- Article
- ISSN
- 0021-8995
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A water-insoluble enzyme was prepared by immobilizing lipoprotein lipase (LPL) onto the surface of the copoly(ethylene/acrylic acid) fine fiber by covalent fixation. The relative activity (RA) of the immobilized LPL was found to remain high toward small ester substrates, p-nitrophenyl laurate (pNPL)
## Abstract __Candida rugosa__ lipase was immobilized on aminoβfunctionalized magnetic supports via crossβlinked enzyme aggregates (CLEA) and used to enhance the enzymatic degradation of polycaprolactone (PCL). The maximum amounts of lipase immobilized on the magnetic beads using glutaraldehyde as