Synthesis of protein‐containing polymers in organic solvents

  title={Synthesis of protein‐containing polymers in organic solvents},
  author={Z. Yang and D. Williams and Alan J. Russell},
  journal={Biotechnology and Bioengineering},
Subtilisin has been modified with polyethylene glycol (PEG) monomethacrylate (MW 8000) by reductive alkylation, and incorporated into polymethyl methacrylate durring free‐radical initiated polymerization. The activity and stability of the PEG‐modified enzymes have been determined in aqueous buffer and organic solvents. The Km and Vmax values for unmodified, singly and doubly modified subtilisin were compared in these environments, and the half‐lives of both modified enzymes were remarkably high… 
Covalent binding of a nerve agent hydrolyzing enzyme within polyurethane foams
A phosphotriesterase preparation, extracted from Escherichia coli DH5α cells, was immobilized within a polyurethane foam matrix during polymer synthesis and analysis of the hydrolysis of paraoxon in aqueous solution demonstrated that more than 50% of the initial enzyme specific activity was retained after immobilization in the foam.
Activity, stability, and conformation of methoxypoly(ethylene glycol)-subtilisin at different concentrations of water in dioxane.
The transesterification activity, autolysis, thermal stability and conformation of subtilisin Carlsberg, made soluble in dioxane by covalent linking to methoxypoly(ethylene glycol) (PEG), were
Synthesis and characterization of hydrophobic ferritin proteins
Chemically stabilized subtilisins in peptide synthesis
Alcalase was 4.6-fold more stable than SC at 65oC and was more tolerant of acetone, acetonitrile and 1,4-dioxane, and compared native alcalase and SC in terms of thermal stability, tolerance of organic solvents and autolysis.
The authors' data demonstrated that the initial rapid deactivation of immobilized DFPase lead to the formation of a hyper-stable and still active form of enzyme, which was investigated in three categories of bioplastic matrices.
Reactivity of temperature‐sensitive, protein‐conjugating polymers prepared by a photopolymerization process
This study was carried out to characterize the reactivity of temperature-sensitive, protein-conjugating polymers prepared by a photopolymerization process. Polymers were based on
Performance of chloroperoxidase stabilization in mesoporous sol-gel glass using In situ glucose oxidase peroxide generation
A unique mesoporous sol-gel glass possessing a highly ordered porous structure (with three pore sizes of about 50, 150, and 200 Å diameter) was used as a support material for immobilization of the
Polyacrylamides as Immobilization Supports for use of Hydrolytic Enzymes in Organic Media
Polyacrylamide beads and celite were used for immobilization of bovine α-chymotrypsin and lipase B from Candida antarctica andLeveling off of the enzyme activity above a certain enzyme loading of the supports indicated mass transfer limitations.


Enzymatic peptide synthesis in organic solvent mediated by gels of copolymerized acrylic derivatives of alpha-chymotrypsin and polyoxyethylene.
Copolymers of acrylated derivatives of alpha-chymotrypsin and polyethylene glycol (PEG) have been prepared and used as biocatalysts for the synthesis of model peptides in organic solvent containing a
Lipase Modified for Solubility in Organic Solvents
Les proteines modifiees par le PEG sont par immunogenes et ont une duree de vie allongee, fixant ainsi sur la lipase de Candida rugosa, des molecules de PEG de longueur differente.
Enzyme structure and mechanism
This is the second edition of this biological reference aimed at undergraduates and graduates. The book covers the structure and mechanism of enzymes, creating a guide to the current understanding of