Enzymatic surface modification lipases

Very few reports are available for the enzymatic surface modification of synthetic fibers. Peroxidase, lipase, cutinase, nitrilase, nitrile hydratase, amidase, protease, and hydrolase have been reported for the surface modification of synthetic polymers (Table 4.1). 

Zeolite membranes are amenable by surface modification with a variety of chemical functional groups using simple silane chemistry that may provide alternative surface chemistry pathways for enzyme immobilization. In this context, Shukla et al. [338] have recently used a chemically modified zeolite-clay composite membrane for the immobilization of porcine lipase using glutaraldehyde to provide a chemical linkage between the enzyme and the membrane. The effects of pH, temperature, and solvent on the performance of such biphasic zeolite-membrane reactors have been evaluated in the hydrolysis of olive oil to fatty acids. Similarly, Algieri et al. [339] have immobilized tyrosinase on FAU membranes for the enzymatic conversion of the 1-tyrosine to 1-DOPA as an effective drug for Parkinson s disease treatment. This approach combines the active role of zeolite membrane as enzyme support and inhibitor suppressor. Moreover,... 

Recently, a new approach using enzymes to modify material (or nanomaterial) surfaces has been developed. This approach utilizes enzymatic hydrolysis or degradation to mildly etch the material surfaces and thus CTeate desirable surface structures or properties [45]. Many polymers, including polyvinyl chloride (PVC), polyaayloni-trile, polyethylene terephthalate, and polyamides, have been modified by this method. In a recent study, PVC tubes were soaked in Rhizopus arrhizus lipase to create nanometer surface features that exhibited antibacterial properties [60]. Enzymatic modification demonstrates great potential and promise for biomedical and nanomedicine applications due to its biocompatible, environmentally friendly, and simple process. 

Alternatively, surface hydrolysis of PET can be achieved by treatment with enzymes that introduce polar groups to the polymer surface. A number of hydrolytic enzymes, such as lipases, cutinases, and esterases, have shown potential for surface functionalization of PET [36, 99]. The biocatalytic method can be performed under mild reaction conditions avoiding the use of large amounts of chemicals and energy for the finishing and dyeing processes. The enzymatic modifications are specific and can be limited to the polymer surface. Consequently, the bulk properties and mechanical stability of the polymer are not compromised, and material savings and products of better quality or with new functionalities can be obtained. 

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