Surface Modification of Cellulose Acetate with Cutinase and ...

Surface Modification of Cellulose Acetate with Cutinase and Cutinase Fused to Carbohydrate-binding Modules
were competitively dyed at 60º C. Relative protein adsorption was calculated as
P
P
0h
0hcutinase
− P
− P
18h
18hcutinase
4. Concluding remarks
and relative K/S was calculated as
K / S
K / S
enzyme
cutinase
− K / S
− K / S
The biomodification of the surface of cellulose acetate with high degree of substitution
with cutinase was demonstrated by the acetic acid release and the improvement in the
chemically specific staining of the fabrics with a reactive dye. From the acetic acid
release, the hydrolysis yield is higher for the less substituted cellulose acetate fabric, but
the consequences of the acetyl hydrolysis are more pronounced for CTA, as shown by
the differences in colour, morphology of the fibres surface and crystallinity between
controls and treated samples. Further studies will be necessary to evaluate the impact of
cutinase activity in the physical properties of the fabrics and to assess the contribution
of the incomplete protein removal and of the physical, rather than chemical,
modifications on the differences seen upon enzymatic treatment.
The design of hybrid enzymes mimics the strategies that nature uses to evolve and it is a
powerful tool in biotechnology. The production and application of the cutinase fused to
CBMs, especially to the fungal CBM of CBHI of T. reesei, provided strong evidences
of being an interesting strategy to pursuit. Future work is needed to improve the
recombinant production of modular cutinases and to study in detail their affinities
toward the cellulose acetates.
From the above considerations, it could be suggested that the cutinase has potential in
textile industry for the surface modification and consequently on the “bicomponent
yarns/fibres” production of cellulose acetate.
control
control
.
153