Immobilization of formaldehyde dehydrogenase in tailored siliceous mesostructured cellular foams and evaluation of its activity for conversion of formate to formaldehyde
Artikel i vetenskaplig tidskrift, 2018

Formaldehyde dehydrogenase (FaldDH) is used as a catalyst to reduce formate to formaldehyde in a cascade reaction to convert CO 2 to methanol. This enzyme, however, has low activity and is sensitive to substrate/product concentration and pH. To improve the performance of FaldDH, it can be immobilized through physical adsorption in siliceous mesostructured cellular foams (MCF), which physical properties are suitable for the immobilization of large molecules as FaldDH (molecular size of 8.6 × 8.6 × 19 nm). In this work two MCF materials were synthesized: MCF1 with a pore size of 26.8 nm and window size of 10.5 nm; and MCF2 with a pore size of 32.9 nm and window size of 13.0 nm. The surfaces of the materials were functionalized with octyl, mercaptopropyl or chloromethyl groups. FaldDH was successfully immobilized inside all the materials, yielding enzyme loadings of about 300 mg g ‐1 in MCF1 and more than 750 mg g −1 in MCF2. However, the enzyme was inactive upon immobilization on MCF1, whereas on MCF2 the enzyme retained its catalytic activity presumably owing to the larger pores of this material and the need for the enzyme to undergo configurational changes during the reaction. Using MCF2 functionalized with mercaptopropyl groups the activity of FaldDH was enhanced beyond that of the free enzyme. Additionally, low leakage of the enzyme from the MCF2 was observed during the reactions. Thus, tailored MCF is a highly attractive material for employment of the FaldDH enzyme.

Mesoporous silica

Enzyme adsorption

Biocatalysis

Formaldehyde dehydrogenase

CO2 reduction

Författare

Milene Zezzi Do Valle Gomes

Kemi och kemiteknik, Tillämpad kemi, Teknisk ytkemi

Anders Palmqvist

Chalmers, Kemi och kemiteknik, Tillämpad kemi

Colloids and Surfaces B: Biointerfaces

0927-7765 (ISSN)

Vol. 163 41-46

Ämneskategorier

Materialkemi

Biokatalys och enzymteknik

Organisk kemi

DOI

10.1016/j.colsurfb.2017.11.069