Nanoclays for Lipase Immobilization: Biocatalyst Characterization and Activity in Polyester Synthesis


Ozturk H., POLLET E., PHALIP V., GUEVENILIR Y., AVEROUS L.

POLYMERS, vol.8, no.12, 2016 (SCI-Expanded) identifier identifier

  • Publication Type: Article / Article
  • Volume: 8 Issue: 12
  • Publication Date: 2016
  • Doi Number: 10.3390/polym8120416
  • Journal Name: POLYMERS
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Keywords: Candida antarctica lipase B, immobilization, sepiolite, montmorillonite, organoclay, epsilon-caprolactone polymerization, CANDIDA-ANTARCTICA, ENZYME IMMOBILIZATION, POLYPROPYLENE POWDER, HYDROPHOBIC SUPPORTS, MODIFIED BENTONITE, CATALYTIC-ACTIVITY, CROSS-LINKING, ADSORPTION, PROTEINS, GLUTARALDEHYDE
  • Istanbul Technical University Affiliated: Yes

Abstract

The immobilization of Candida antarctica lipase B (CALB) was performed by physical adsorption on both neat and organo-modified forms of sepiolite and montmorillonite. The influence of different parameters, e.g., solvent, enzyme loading, cross-linking, and type of clay support, on immobilization efficiency and catalyst hydrolytic activity has been investigated. The highest hydrolytic activities were obtained for CALB immobilized on organo-modified clay minerals, highlighting the beneficial effect of organo-modification. The esterification activity of these CALB/organoclay catalysts was also tested in the ring-opening polymerization of epsilon-caprolactone. The polymerization kinetics observed for clay-immobilized catalysts confirmed that CALB adsorbed on organo-modified montmorillonite (CALB/MMTMOD) was the highest-performing catalytic system.