Immobilization ofCandida antarcticaLipase on Nanomaterials and Investigation of the Enzyme Activity and Enantioselectivity

Coskun G., Ciplak Z., Yildiz N., Mehmetoglu U.

APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY, cilt.193, sa.2, ss.430-445, 2021 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 193 Sayı: 2
  • Basım Tarihi: 2021
  • Doi Numarası: 10.1007/s12010-020-03443-2
  • Dergi Adı: APPLIED BIOCHEMISTRY AND BIOTECHNOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, PASCAL, Agricultural & Environmental Science Database, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, Biotechnology Research Abstracts, CAB Abstracts, Chemical Abstracts Core, Compendex, EMBASE, Food Science & Technology Abstracts, MEDLINE, Pollution Abstracts, Veterinary Science Database
  • Sayfa Sayıları: ss.430-445
  • Anahtar Kelimeler: Candida antarcticalipase, Immobilization, Nanoparticles, Enzyme activity, Kinetic resolution, LIPASE-B, KINETIC RESOLUTION, CANDIDA-RUGOSA, MAGNETIC NANOPARTICLES, NANOCOMPOSITES, BIODIESEL, MEMBRANES
  • Sivas Cumhuriyet Üniversitesi Adresli: Evet

Özet

This study defines the lipase immobilization protocol and enzymatic kinetic resolution of 1-phenyl ethanol with the use of immobilized lipases (LI) as a biocatalyst. Commercially available lipaseCandida antarctica B(Cal-B) was immobilized onto graphene oxide (GO), iron oxide (Fe3O4) nanoparticles, and graphene oxide/iron oxide (GO/Fe3O4) nanocomposites. Characterization of pure and enzyme-loaded supports was carried out by scanning electron microscopy (SEM) and Fourier transform infrared (FTIR) spectroscopy. The influences of pH, temperature, immobilization time, crosslinker concentration, glutaraldehyde (GLA), epichlorohydrin (EPH), and surfactant concentrations (Tween 80 and Triton X-100) on the catalytic activity were evaluated for these three immobilized biocatalysts. The highest immobilized enzyme activities were 15.03 U/mg, 14.72 U/mg, and 13.56 U/mg for GO-GLA-CalB, Fe3O4-GLA-CalB, and GO/Fe3O4-GLA-CalB, respectively. Moreover, enantioselectivity and reusability of these immobilized lipases were compared for the kinetic resolution of 1-phenyl ethanol, using toluene as organic solvent and vinyl acetate as acyl donor. The highest values of enantiomeric excess (ee(s) = 99%), enantioselectivity (E = 507.74), and conversion (c = 50.73%) were obtained by using lipase immobilized onto graphene oxide (GO-GLA-CalB). It was obtained that this enzymatic process may be repeated five times without important loss of enantioselectivity.