Rational nanoconjugation improves biocatalytic performance of enzymes: Aldol addition catalyzed by immobilized rhamnulose-1-phosphate aldolase

Inés Ardao, Joan Comenge, M. Dolors Benaiges, Gregorio Álvaro, Víctor F. Puntes

Research output: Contribution to journalArticleResearchpeer-review

35 Citations (Scopus)

Abstract

Gold nanoparticles (AuNPs) are attractive materials for the immobilization of enzymes due to several advantages such as high enzyme loading, absence of internal diffusion limitations, and Brownian motion in solution, compared to the conventional immobilization onto porous macroscopic supports. The affinity of AuNPs to different groups present at the protein surface enables direct enzyme binding to the nanoparticle without the need of any coupling agent. Enzyme activity and stability appear to be improved when the biocatalyst is immobilized onto AuNPs. Rhamnulose-1-phosphate aldolase (RhuA) was selected as model enzyme for the immobilization onto AuNPs. The enzyme loading was characterized by four different techniques: surface plasmon resonance (SPR) shift and intensity, dynamic light scattering (DLS), and transmission electron microscopy (TEM). AuNPs-RhuA complexes were further applied as biocatalyst of the aldol addition reaction between dihydroxyacetone phosphate (DHAP) and (S)-Cbz-alaninal during two reaction cycles. In these conditions, an improved reaction yield and selectivity, together with a fourfold activity enhancement were observed, as compared to soluble RhuA. © 2012 American Chemical Society.
Original languageEnglish
Pages (from-to)6461-6467
JournalLangmuir
Volume28
DOIs
Publication statusPublished - 17 Apr 2012

Fingerprint Dive into the research topics of 'Rational nanoconjugation improves biocatalytic performance of enzymes: Aldol addition catalyzed by immobilized rhamnulose-1-phosphate aldolase'. Together they form a unique fingerprint.

Cite this