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Insight into in situ enzymatic transesterification modification of polyethylene terephthalate fibers with polyethylene glycol.
- Source :
-
Process Biochemistry . Nov2024, Vol. 146, p140-146. 7p. - Publication Year :
- 2024
-
Abstract
- Polyethylene terephthalate (PET) fabric was enzymatically modified with polyethylene glycol (PEG). Lipase from Aspergillus oryzae was used as a catalyst. The wetting behavior of the modified PET fabric was characterized by the water contact angle, water adsorption dynamics and moisture regain. The initial water contact angle of the modified fabric decreased from 129.3° to 74.9°. The water absorption dynamics results indicated that the equilibrium water absorption amount of the modified fabric was approximately 10 times greater than that of the untreated sample. The initial absorption rate (V init) of the modified fabric was almost 30 times higher than that of the untreated fabric. The moisture regain reached 3.52 % after modification. Scanning electron microscopy revealed granular and sheet coatings on the surface of the modified fabric. Chemical linkage of PEG onto the PET fibers was confirmed by attenuated total reflection–Fourier transform infrared spectroscopy. The modification had no significant effect on the thermal properties of the PET fabrics according to the thermogravimetric curve and differential scanning calorimetry results. The mechanical properties of the modified fabric were slightly improved. Therefore, in situ enzymatic transesterification between PET and PEG could be a potential novel modification approach for adding value to PET fiber textiles. [Display omitted] • Polyethylene glycol was chemically linked onto polyethylene terephthalate(PET) fiber. • PET fibers was hydrophilic modified by lipase-catalyzed transesterification reaction. • The water contact angle of modified PET fabric decreased from 129.3° to 74.9°. • The moisture regain of modified PET fabric reached (3.52±0.02)%. • The mechanical properties of PET fabric were slightly improved after modification. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 13595113
- Volume :
- 146
- Database :
- Academic Search Index
- Journal :
- Process Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 180459848
- Full Text :
- https://doi.org/10.1016/j.procbio.2024.07.031