Premium
Enzyme‐Decorated Covalent Organic Frameworks as Nanoporous Platforms for Heterogeneous Biocatalysis
Author(s) -
Oliveira Felipe L.,
Souza Stefania P.,
Bassut Jonathan,
Álvarez Heiddy M.,
GarciaBasabe Yunier,
Alves de Souza Rodrigo O. M.,
Esteves Pierre M.,
Gonçalves Raoni S. B.
Publication year - 2019
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201903807
Subject(s) - covalent bond , nanoporous , candida antarctica , biocatalysis , chemistry , immobilized enzyme , catalysis , adsorption , organic chemistry , selectivity , lipase , oleic acid , enzyme , heterogeneous catalysis , enzyme catalysis , chemical engineering , combinatorial chemistry , biochemistry , ionic liquid , engineering
Sustainability in chemistry heavily relies on heterogeneous catalysis. Enzymes, the main catalyst for biochemical reactions in nature, are an elegant choice to catalyze reactions due to their high activity and selectivity, although they usually suffer from lack of robustness. To overcome this drawback, enzyme‐decorated nanoporous heterogeneous catalysts were developed. Three different approaches for Candida antarctica lipase B (CAL‐B) immobilization on a covalent organic framework (PPF‐2) were employed: physical adsorption on the surface, covalent attachment of the enzyme in functional groups on the surface and covalent attachment into a linker added post‐synthesis. The influence of the immobilization strategy on the enzyme uptake, specific activity, thermal stability, and the possibility of its use through multiple cycles was explored. High specific activities were observed for PPF‐2‐supported CAL‐B in the esterification of oleic acid with ethanol, ranging from 58 to 283 U mg −1 , which was 2.6 to 12.7 times greater than the observed for the commercial Novozyme 435.