Insights into the Interaction between Immobilized Biocatalysts and Metal-Organic Frameworks: A Case Study of PCN-333.

The immobilization of enzymes in metal-organic frameworks (MOFs) with preserved biofunctionality paves a promising way to solve problems regarding the stability and reusability of enzymes. However, the rational design of MOF-based biocomposites remains a considerable challenge as very little is known about the state of the enzyme, the MOF support, and their host-guest interactions upon immobilization. In this study, we elucidate the detailed host-guest interaction for MOF immobilized enzymes in the biointerface.

Influence of the Synthesis and Storage Conditions on the Activity of Lipase B ZIF-8 Biocomposites.

The biomimetic mineralization of zeolitic imidazolate framework-8 (ZIF-8) has been reported as a strategy for enzyme immobilization, enabling the heterogenization and protection of biomacromolecules. Here, we report the preparation of different lipase B biocomposites (CALB@ZIF-8) formed by altering the concentrations of Zn and 2-methylimidazole (2-mIM). The influence of synthetic conditions on the catalytic activity of the lipase CALB was examined by hydrolysis and transesterification assays in aqueous and organic media, respectively.

Enhanced Activity of Enzymes Encapsulated in Hydrophilic Metal-Organic Frameworks.

Encapsulation of biomacromolecules in metal-organic frameworks (MOFs) can preserve biological functionality in harsh environments. Despite the success of this approach, termed biomimietic mineralization, limited consideration has been given to the chemistry of the MOF coating. Here, we show that enzymes encapsulated within hydrophilic MAF-7 or ZIF-90 retain enzymatic activity upon encapsulation and when exposed to high temperatures, denaturing or proteolytic agents, and organic solvents, whereas hydrophobic ZIF-8 affords inactive catalase and negligible protection to urease.

Protein surface functionalisation as a general strategy for facilitating biomimetic mineralisation of ZIF-8.

The durability of enzymes in harsh conditions can be enhanced by encapsulation within metal-organic frameworks (MOFs) a process called biomimetic mineralisation. Herein we show that the surface charge and chemistry of a protein determines its ability to seed MOF growth. We demonstrate that chemical modification of amino acids on the protein surface is an effective method for systematically controlling biomimetic mineralisation by zeolitic imidazolate framework-8 (ZIF-8).

The self-sufficient CYP102 family enzyme, Krac9955, from Ktedonobacter racemifer DSM44963 acts as an alkyl- and alkyloxy-benzoic acid hydroxylase.

A self-sufficient CYP102 family encoding gene (Krac_9955) has been identified from the bacterium Ktedonobacter racemifer DSM44963 which belongs to the Chloroflexi phylum. The characterisation of the substrate range of this enzyme was hampered by low levels of production using E. coli.

Characterisation of two self-sufficient CYP102 family monooxygenases from Ktedonobacter racemifer DSM44963 which have new fatty acid alcohol product profiles.

Background: Two self-sufficient CYP102 family encoding genes (Krac_0936 and Krac_9955) from the bacterium Ktedonobacter racemifer DSM44963, which possesses one of the largest bacterial genomes, have been identified.

Methods: Phylogenetic analysis of both the encoded cytochrome P450 enzymes, Krac0936 and Krac9955. Both enzymes were produced and their turnovers with fatty acid substrates assessed in vitro and using a whole-cell oxidation system.