1.Department of Biomedical and Pharmaceutical Sciences, College of Pharmacy,University of Rhode Island,Kingston,USA;2.Particulate Fluids Processing Centre, School of Chemistry,The University of Melbourne,Melbourne,Australia;3.Department of Life Science Engineering, Faculty of New Sciences and Technologies,University of Tehran,Tehran,Iran;4.Department of Chemistry,University of Zanjan,Zanjan,Iran;5.School of Natural Sciences,Griffith University,Nathan Campus,Australia;6.Faculty of Pharmacy,Shahid Sadoughi University of Medical Sciences,Yazd,Iran;7.Division of Microbiology, Department of Pathobiology, School of Public Health,Tehran University of Medical Sciences sTUMS,Tehran,Iran;8.Biosensor Research Center, Endocrinology and Metabolism Molecular-Cellular Sciences Institute,Tehran University of Medical Sciences,Tehran,Iran;9.Nanobiomaterials Group, Pharmaceutical Sciences Research Center,Tehran University of Medical Sciences,Tehran,Iran;10.Department of Pharmaceutical Biotechnology, Faculty of Pharmacy and Biotechnology Research Center,Tehran University of Medical Sciences,Tehran,Iran;11.Department of Pharmaceutical Biomaterials and Medical Biomaterials Research Center, Faculty of Pharmacy,Tehran University of Medical Sciences,Tehran,Iran
Abstract:
An enzyme immobilized on a mesoporous silica nanoparticle can serve as a multiple catalyst for the synthesis of industrially useful chemicals. In this work, MCM-41 nanoparticles were coated with polyethylenimine (MCM-41@PEI) and further modified by chelation of divalent metal ions (M = Co2+, Cu2+, or Pd2+) to produce metal-chelated silica nanoparticles (MCM-41@PEI-M). Thermomyces lanuginosa lipase (TLL) was immobilized onto MCM-41, MCM-41@PEI, and MCM-41@PEI-M by physical adsorption. Maximum immobilization yield and efficiency of 75 ± 3.5 and 65 ± 2.7% were obtained for MCM@PEI-Co, respectively. The highest biocatalytic activity at extremely acidic and basic pH (pH = 3 and 10) values were achieved for MCM-PEI-Co and MCM-PEI-Cu, respectively. Optimum enzymatic activity was observed for MCM-41@PEI-Co at 75 °C, while immobilized lipase on the Co-chelated support retained 70% of its initial activity after 14 days of storage at room temperature. Due to its efficient catalytic performance, MCM-41@PEI-Co was selected for the synthesis of ethyl valerate in the presence of valeric acid and ethanol. The enzymatic esterification yield for immobilized lipase onto MCM-41@PEI-Co was 60 and 53%, respectively, after 24 h of incubation in n-hexane and dimethyl sulfoxide media.
Graphical Abstract Divalent metal chelated polyethylenimine coated MCM-41 (MCM-41@PEI-M) was used for immobilization of Thermomyces lanuginosa lipase catalyzing green apple flavor preparation
