4.6 Article

In-situ lipase-catalyzed cotton coating with polyesters from ethylene glycol and glycerol

Journal

PROCESS BIOCHEMISTRY
Volume 66, Issue -, Pages 82-88

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.procbio.2018.01.002

Keywords

Immobilized Candida antarctica lipase B; Polymerization; Conversion rate; Lipase from Thermomyces lanuginosus; In situ lipase-catalyzed polymerization; Cotton

Funding

  1. Chinese government scholarship [201706790049]
  2. Jiangsu Province Scientific Research Innovation Project for Academic Graduate Students [KYLX16_0788]
  3. Training Fund for Excellent Doctoral Student in Jiangnan University
  4. Key Projects of governmental cooperation in international scientific and technological innovation [2016 YFE0115700]
  5. National Key R & D Program of China [2017 YFB0309100]
  6. Portuguese Foundation for Science and Technology (FCT) [UID/BIO/04469/2013, POCI-01-0145-FEDER-006684, RECI/BB-EBI/0179/2012, FCOMP-1-0124-FEDER-027462]
  7. BioTecNorte operation - European Regional Development Fund under Norte - Programa Operacional Regional do Norte [NORTE-01-0145-FEDER-00004]
  8. National Natural Science Foundation of China [31470509, 31201134]
  9. Industry-Academic Joint Technological Prospective Fund Project of Jiangsu Province [BY2013015-24, BY2016022-23]
  10. fundamental research funds for the central universities [JUSRP 51622A]
  11. Priority Academic Program Development of Jiangsu Higher Education Institutions

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Several polyesters were synthesized from ethylene glycol, glycerol and adipate, succinate dimethyl esters. Immobilized Candida antarctica lipase B was used as catalyst for 6 h under vacuum at 70 degrees C without any further solvents. The highest conversion rate of 88.5% occurred for the polymerization of poly(ethylene adipate), evaluated by H-1 NMR. MALDI-TOF analysis indicated that most of the oligomers formed were dimers or tamers. After successfully synthesize the polyesters we set-up the optimal conditions for their in-situ coating onto cotton substrates with a soluble lipase from Thermomyces lanuginosus. This work presents a novel bio-approach to impart hydrophobic properties to coated cotton-based fibre materials.

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