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Investigations on vinylene carbonate. V. Immobilization of alkaline phosphatase onto LDPE films cografted with vinylene carbonate and N ‐vinyl‐ N ‐methylacetamide
Author(s) -
Chen Guohua,
van der Does Leen,
Bantjes Adriaan
Publication year - 1993
Publication title -
journal of applied polymer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.575
H-Index - 166
eISSN - 1097-4628
pISSN - 0021-8995
DOI - 10.1002/app.1993.070470105
Subject(s) - low density polyethylene , alkaline phosphatase , diethylenetriamine , polyethylene , covalent bond , polymer chemistry , chemistry , immobilized enzyme , nuclear chemistry , bovine serum albumin , carbonate , matrix (chemical analysis) , materials science , enzyme , chromatography , organic chemistry
Low‐density polyethylene (LDPE) films cografted with vinylene carbonate (VCA) and N ‐vinyl‐ N ‐methylacetamide (VIMA) were studied as a matrix for the immobilization of the enzyme alkaline phosphatase (ALP) either by direct fixation or by inserting spacers. When water‐soluble alkyldiamines such as diaminoethylene, diaminobutane, diethylenetriamine, and diaminohexane were used as spacers between the matrix and the enzyme, the surface concentration (SC) of the active ALP coupled on the matrix was increased, whereas the effect of the spacer on the SC was dependent on the length of the spacer. Bovine serum albumin (BSA) was preimmobilized onto the LDPE films to provide a better simulation of the biological environment for the enzyme, and the SC of ALP on the matrix was significantly increased by coupling ALP onto the BSA preimmobilized surfaces. Compared to native ALP, some physicochemical properties of ALP could be improved by the covalent immobilization. © 1993 John Wiley & Sons, Inc.

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