Affiliations 

  • 1 Department of Chemistry, Faculty of Science, Universiti Teknologi Malaysia (UTM), 81310, Johor Bahru, Johor, Malaysia; Department of Applied Chemistry, Federal University Dutsin-Ma (FUDMA), P.M.B. 5001, Dutsin-Ma, Katsina State, Nigeria; Enzyme Technology and Green Synthesis Group, Faculty of Science, Universiti Teknologi Malaysia (UTM), 81310, Johor Bahru, Johor, Malaysia
  • 2 Department of Chemistry, Faculty of Science, Universiti Teknologi Malaysia (UTM), 81310, Johor Bahru, Johor, Malaysia; Enzyme Technology and Green Synthesis Group, Faculty of Science, Universiti Teknologi Malaysia (UTM), 81310, Johor Bahru, Johor, Malaysia. Electronic address: roswanira@kimia.fs.utm.my
  • 3 Department of Chemistry, Faculty of Science, Universiti Teknologi Malaysia (UTM), 81310, Johor Bahru, Johor, Malaysia; Enzyme Technology and Green Synthesis Group, Faculty of Science, Universiti Teknologi Malaysia (UTM), 81310, Johor Bahru, Johor, Malaysia
Enzyme Microb Technol, 2021 Aug;148:109807.
PMID: 34116744 DOI: 10.1016/j.enzmictec.2021.109807

Abstract

Oil palm leaves (OPL) silica (SiO2) can replace the energy-intensive, commercially produced SiO2. Moreover, the agronomically sourced biogenic SiO2 is more biocompatible and cost-effective enzyme support, which properties could be improved by the addition of magnetite (Fe3O4) and graphene oxide (GO) to yield better ternary support to immobilize enzymes, i.e., Candida rugosa lipase (CRL). This study aimed to optimize the Candida rugosa lipase (CRL immobilization onto the ternary OPL-silica-magnetite (Fe3O4)-GO (SiO2/Fe3O4/GO) support, for use as biocatalyst for ethyl valerate (EV) production. Notably, this is the first study detailing the CRL/SiO2/Fe3O4/GO biocatalyst preparation for rapid and high yield production of ethyl valerate (EV). AFM and FESEM micrographs revealed globules of CRL covalently bound to GL-A-SiO2/Fe3O4/GO; similar to Raman and UV-spectroscopy results. FTIR spectra revealed amide bonds at 3478 cm-1 and 1640 cm-1 from covalent interactions between CRL and GL-A-SiO2/Fe3O4/GO. Optimum immobilization conditions were 4% (v/v) glutaraldehyde, 8 mg/mL CRL, at 16 h stirring in 150 mM NaCl at 30 °C, offering 24.78 ± 0.26 mg/g protein (specific activity = 65.24 ± 0.88 U/g). The CRL/SiO2/Fe3O4/GO yielded 77.43 ± 1.04 % of EV compared to free CRL (48.75 ± 0.70 %), verifying the suitability of SiO2/Fe3O4/GO to hyperactivate and stabilize CRL for satisfactory EV production.

* Title and MeSH Headings from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.