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Lipoprotein Lipase Immobilization onto Porous Chitosan Beads
Author(s) -
Itoyama Koki,
Tokura Seiichi,
Hayashi Toshio
Publication year - 1994
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp00026a013
Subject(s) - lipoprotein lipase , immobilized enzyme , chemistry , chitosan , covalent bond , lipase , substrate (aquarium) , thermal stability , chromatography , enzyme , organic chemistry , oceanography , geology
Lipoprotein lipase (LPL) was covalently immobilized onto the surface of porous chitosan beads (ChB) without or with spacers of different lengths. The relative activity (RA) of the immobilized LPL was found to be high toward a small ester substrate, p ‐nitrophenyl laurate (pNPL). LPL immobilized with spacer gave an almost constant activity, in marked contrast with the immobilized LPL without spacer, whose activity decreased with decreasing surface concentration. Further, the RA of LPL immobilized with spacer was higher than that of LPL immobilized without a spacer. The pH, thermal, and storage stabilities of the immobilized LPL were higher than those of the free one. LPL immobilized directly to the surface of ChB without any spacer gave a higher stability than that immobilized with spacer, in spite of the lower RA. The spacer effect on RA could be explained in terms of the mobility of the immobilized LPL molecule.