Metal-Chelate Immobilization of Lipase Onto Polyethylenimine Coated Mcm-41 for Apple Flavor Synthesis Publisher Pubmed



Sadighi A¹ ; Motevalizadeh SF² ; Hosseini M³ ; Ramazani A⁴ ; Gorgannezhad L⁵ ; Nadri H⁶ ; Deiham B⁷ ; Ganjali MR⁸ ; Shafiee A⁹ ; Faramarzi MA¹⁰ ; Khoobi M^{9, 11} Show Affiliations
Source: Applied Biochemistry and Biotechnology Published:2017

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. [Figure not available: see fulltext.]. © 2017, Springer Science+Business Media New York.