Investigations on vinylene carbonate. V. Immobilization of alkaline phosphatase onto LDPE films cografted with vinylene carbonate and N‐vinyl‐N‐methylacetamide

Abstract

SYNOPSISLow-density polyethylene (LDPE) films cografted with vinylene carbonate (VCA) and Nvinyl-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.

Removal of alkylphenols by the combined use of tyrosinase immobilized on ion‐exchange resins and chitosan beads

“…Ion-exchange resins immobilized with tyrosinase were packed in one column, and chemically crosslinked chitosan beads prepared with ECH were packed in another column. The enzymatic activity of tyrosinase was modified by the covalent immobilization, and immobilized tyrosinase had a high activity in the temperature range of [30][31][32][33][34][35][36][37][38][39][40][41][42][43][44][45] C and the pH range of 7-9. When a p-cresol solution was circulated through the two columns packed with tyrosinase-immobilized ion-exchange resins and crosslinked chitosan beads at 45 C and pH 7.0, p-cresol was effectively removed by quinone oxidation with immobilized tyrosinase and subsequent quinone adsorption on chitosan beads.…”

“…In general, such a support should display the following properties: a hydrophilic nature, an appropriate concentration of reactive functional groups, resistance to biodegradation, and chemical and mechanical stability. [31][32][33] In addition, the covalent binding of enzymes on waterinsoluble supports is required to be carried out under mild conditions to avoid considerable inactivation of the enzymes. Covalent immobilization involves the reaction between functional groups present in the polymeric supports and the functional ones in the enzymes.…”

Synthesis of soluble poly(vinylene carbonate) by redox-initiated RAFT process in microemulsion and its aminolysis yielding snow-white polymethylol

“…A number of cyclic carbonate functional vinyl monomers have been prepared from their corresponding epoxy monomers, such as glycidylmethacrylate, 3 glycidylacrylate 4 glycidyl vinyl ether 5 and 3-butene-1,2-diol, 6 by the action of carbon dioxide or diethyl carbonate. [11][12][13] Another interesting monomer is vinylene carbonate (VCB), whose polymers and copolymers have similar applications. [7][8][9] One major application of polymers with cyclic carbonate groups is based on their rapid reaction with amines, yielding hydroxyurethane moieties at room temperature.…”

Poly(vinyl alcohol) based monomers for lithography-based 3D fabrication

“…Alkaline phosphatase (ALP) was used as a model protein, because of its enzymatic properties, which enable quantitative information on the amount of bound protein, as well as determination of enzyme bioactivity. With regard to the ethylene carbonate or propylene carbonate functionalities, TRIS buffer (pH 8.5) has been recommended in the literature (7).…”

“…In order to enable surface modification via covalent protein attachment, resins that have shown promising results as potential scaffold material (vinyl ester) were made aminoreactive by incorporation of cyclic carbonate moieties that have well documented affinity towards free amine groups-VEC (Vinylene carbonate) und PCVC (4 (Hydroxymethyl)-1,3-dioxolan-2-one vinyl carbonate) (7,8,9). Alkaline phosphatase (ALP) was used as a model protein, because of its enzymatic properties, which enable quantitative information on the amount of bound protein, as well as determination of enzyme bioactivity.…”