Pseudomonas fluorescens lipase (Pfl) was adsorbed on macroporous polypropylene to obtain a heterogeneous biocatalyst. The effect of NaCl concentration and of different 100 mm sodium salts on the Pfl loading and catalytic performance toward biodiesel synthesis via the solvent-free methanolysis of triglycerides was studied. Although lipase adsorption onto polypropylene is governed by hydrophobic interactions, both salt concentration and anion type affect lipase loading. Protein loading decreased along the series: Cl- > SO42- ≈ no salt > Br- > I- > SCN- > F- > AcO-. This nonmonotonic ion-specific trend can be the result of opposite mechanisms occurring during the adsorption step. A similar trend is observed also for triglyceride conversion and biodiesel yield. It is likely that ions affect the microenvironment of the adsorbed lipase by interacting specifically with the hydration water and polypeptide chains, thus affecting enzyme catalysis.

Specific Anion Effects on Lipase Adsorption and Enzymatic Synthesis of Biodiesel in Nonaqueous Media

Carucci, Cristina
Secondo
;
Salis, Andrea
Ultimo
2020-01-01

Abstract

Pseudomonas fluorescens lipase (Pfl) was adsorbed on macroporous polypropylene to obtain a heterogeneous biocatalyst. The effect of NaCl concentration and of different 100 mm sodium salts on the Pfl loading and catalytic performance toward biodiesel synthesis via the solvent-free methanolysis of triglycerides was studied. Although lipase adsorption onto polypropylene is governed by hydrophobic interactions, both salt concentration and anion type affect lipase loading. Protein loading decreased along the series: Cl- > SO42- ≈ no salt > Br- > I- > SCN- > F- > AcO-. This nonmonotonic ion-specific trend can be the result of opposite mechanisms occurring during the adsorption step. A similar trend is observed also for triglyceride conversion and biodiesel yield. It is likely that ions affect the microenvironment of the adsorbed lipase by interacting specifically with the hydration water and polypeptide chains, thus affecting enzyme catalysis.
File in questo prodotto:
File Dimensione Formato  
2020 acs.langmuir.0c01330.pdf

Solo gestori archivio

Descrizione: articolo principale
Tipologia: versione editoriale (VoR)
Dimensione 1.61 MB
Formato Adobe PDF
1.61 MB Adobe PDF   Visualizza/Apri   Richiedi una copia

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11584/294667
Citazioni
  • ???jsp.display-item.citation.pmc??? 0
  • Scopus 10
  • ???jsp.display-item.citation.isi??? 10
social impact