Immobilization of Candida rugosa lipase on magnetic chitosan beads and application in flavor esters synthesis


FOOD CHEMISTRY, vol.366, 2022 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 366
  • Publication Date: 2022
  • Doi Number: 10.1016/j.foodchem.2021.130699
  • Journal Name: FOOD CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, PASCAL, Aerospace Database, Aquatic Science & Fisheries Abstracts (ASFA), BIOSIS, CAB Abstracts, Chimica, Communication Abstracts, Compendex, EMBASE, Food Science & Technology Abstracts, MEDLINE, Metadex, Veterinary Science Database, Civil Engineering Abstracts
  • Keywords: Magnetic chitosan beads, Candida rugosa Lipase, Immobilized enzyme, Ester synthesis, Enzyme kinetics, THERMOMYCES-LANUGINOSUS LIPASE, ENZYMATIC-SYNTHESIS, ADSORPTION, ESTERIFICATION, NANOPARTICLES, OPTIMIZATION
  • Gazi University Affiliated: Yes


In this work, magnetic chitosan (MCH) beads were synthesized by phase-inversion method, and grafted with polydopamine (PDA) and then used for direct immobilization of Candida rugosa lipase by Schiff base reaction. The amount of immobilized enzyme and the retained activity were found to be 47.3 mg/g and 72.8%, respectively, at pH 7.0, and at 25 degrees C. The apparent Km (9.7 mmol/L), and Vmax (384 U/mg) values of the immobilized lipase were significantly changed compared to the free lipase. The MCH@PDA-lipase was better thermal and storage stability at different temperatures than those of the free lipase. In hexane medium, the esterification reaction results showed that the maximum conversions of isoamylalcohol and isopentyl alcohol to isoamyl acetate and isopentyl acetate using the MCH@PDA-lipase were found to be 98.4 +/- 1.3% and 73.7 +/- 0.7%, respectively. These results showed that the MCH@PDA-lipase can be used as an operative immobilized enzyme system for many biotechnological applications.