Polyester coating of cellulose fiber surfaces catalyzed by a cellulose-binding module-Candida antarctica lipase B fusion protein.
A new approach to introduce polymers to cellulosic materials was developed by using the ability of a cellulose-binding module-Candida antarctica lipase B conjugate to catalyze ring-opening polymerization of epsilon-caprolactone in close proximity to cellulose fiber surfaces. The epsilon-caprolactone was introduced to the cellulose surfaces either by simple addition of liquid monomer or through gas phase. The effects of water activity and temperature on the lipase-catalyzed polymerization process were investigated. Analysis showed that the water content in the system primarily regulated the obtained polymer molecular weight, whereas the temperature influenced the reaction rate. The hydrophobicity of the obtained surfaces did not arise from covalent attachment of the poly(epsilon-caprolactone) to the surface hydroxyl groups but rather from surface-deposited polymers which could be readily extracted. The degree of lipase-catalyzed hydrolysis through introduction of water to the polymer-coated cellulose fiber surfaces was also investigated and shown to be significant.
Gustavsson
Malin T
MT
Royal Institute of Technology, Department of Biotechnology, AlbaNova University Centre, SE-106 91 Stockholm, Sweden.
Persson
Per Valdemar
PV
Iversen
Tommy
T
Hult
Karl
K
Martinelle
Mats
M
D002175:Candida / Q000201:enzymology; D002384:Catalysis; D002482:Cellulose / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000737:chemistry / Q000378:metabolism; D005656:Fungal Proteins; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D011091:Polyesters / Q000737:chemistry*; D013499:Surface Properties
D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D011091:Polyesters; D002482:Cellulose; D008049:Lipase; C431349:lipase B, Candida antarctica