Embodiments of the present disclosure relate to methods, compositions, and systems for proximity-based, photoactivated labeling of molecules. Molecules may be labeled via activation of a ligated photocatalyst capable of transmitting energy to a proximal biomolecular labeling agent. Depending on the activated half-life and diffusion coefficient of the labeling agent, molecules within a particular vicinity of the ligated photocatalyst may be labeled but molecules outside the vicinity will not be labeled.

Provided herein are vesicular nanocatalysts decorated on their surface with enzymes, such as for industrial use. More particularly, the nanocatalysts include outer membrane vesicles (OMVs) presenting on their surface carbonic anhydrase or a functional fragment or derivative thereof. Uses, methods of manufacture, and compositions of the nanocatalysts are also disclosed herein.

Provided are compositions that include a metal-organic framework (MOF) including a framework defining an internal volume, an enzyme disposed within the internal volume, and a surfactant. Also provided are methods of making the compositions and their use.

Discovery of the first rare earth-dependent enzyme in methylotrophic M. extorquens AM1 prompted research toward understanding the unique chemistry at play in these systems. This enzyme, an alcohol dehydrogenase (ADH), features a La.sup.3+ ion closely associated with redox-active coenzyme pyrroloquinoline quinone (PQQ). AM1 also produces a periplasmic PQQ-binding protein characterized by a Lys residue hydrogen-bonded to PQQ. Accordingly, we prepared K.sub.115A-, and K.sub.115D-PqqT variants to assess the relevance of this site toward metal binding. Isothermal titration calorimetry experiments, and titrations monitored by UV-vis absorption and emission spectroscopies support that K.sub.115D-PqqT binds tightly (K.sub.d=0.60.2 M) to La.sup.3+ in the presence of bound PQQ and produces spectral signatures consistent with those of ADH enzymes. Addition of benzyl alcohol to La.sup.3+-bound PQQK.sub.115D-PqqT produces spectroscopic changes associated with PQQ reduction, and chemical trapping experiments reveal the production of benzaldehyde, supporting ADH activity.

A fully-continuous synthesis method of cyproterone acetate is provided. 4-androstene-3,17-dione is adopted as a starting material. The present disclosure adopts a fully continuous device composed of micromixers, microreactors, online gravity separation units, online solvent switching units, online solvent concentration units and solvent recovery systems connected according to a cyproterone acetate synthesis route. Cyproterone acetate product is synthesized through one enzymatic catalytic reaction, nine chemical reactions and continuous operations. This can realize recovery of dichloromethane, dichloroethane and ethanol, and significantly reduce emission of three wastes. The obtained crude cyproterone acetate is subjected to decolorization, recrystallization, filtration and drying to obtain pure cyproterone acetate with a purity greater than 99%.

The present disclosure relates to a porous liquid or a porous liquid enzyme system that includes a high surface area solid and a liquid film substantially covering the high surface area solid. The porous liquid or porous liquid enzyme may be contacted with a fluid that is immiscible with the liquid film such that a liquid-fluid interface is formed. The liquid film may facilitate mass transfer of a substance or substrate across the liquid-fluid interface. The present disclosure also provides methods of performing liquid-based extractions and enzymatic reactions utilizing the porous liquid or porous liquid enzyme of the present disclosure. The present disclosure also provides methods for selecting the components of the porous liquid or a porous liquid enzyme system and methods of self-replenishing the used liquid coating.