Aldolases are seen as an attractive route to the production of biologically important compounds due to their ability to form carbon-carbon bonds. However, for many industrial reactions there are no naturally occurring enzymes, and so many different engineering approaches have been used to address this problem. Engineering methods have been used to alter the stability, substrate specificity and ...

Can in silico engineering speed up the delivery of biocatalysts for the burgeoning bioeconomy? In this issue, Kamerlin and coworkers introduce CADEE [Amrein et al. (2017), IUCrJ, 4, 50-64] - a framework for Computer-Aided Directed Evolution of Enzymes - that promises to lessen the burden on 'wet lab' enzymologists when optimizing biocatalysts using laboratory-based directed evolution methods.

Lipases have received great attention as industrial biocatalysts in areas like oils and fats processing, detergents, baking, cheese making, surface cleaning, or fine chemistry [1,2]. They can catalyse reactions of insoluble substrates at the lipid-water interface, preserving their catalytic activity in organic solvents [3]. This makes of lipases powerful tools for catalysing not only hydrolysis...

No. Mei0279 Imaging the Distribution and Secondary Structure of Enzymes on Different Matrixes Using Infrared Microspectroscopy Ying Mei, Yong Chen, Richard Gross (Polytechnic Univ.) and Lisa Miller (NSLS) Beamline(s): U10B Introduction: Enzymes catalyze a plethora of reactions with high specificity, speed, and yield. However, in order to be useful as industrial biocatalysts, improvements in enz...

BACKGROUND Biocatalytic asymmetric reductions with whole cells can offer high enantioselectivity, environmentally benign processes and energy-effective operations and thus are of great interest. The application of whole cell-mediated bioreduction is often restricted if substrate and product have low water solubility and/or high toxicity to the biocatalyst. Many studies have shown that a biphasi...

Esterases, lipases, and serine proteases have been applied as versatile biocatalysts for preparing a variety of chiral compounds in industry via the kinetic resolution of their racemates. In order to meet this requirement, three approaches of enzyme engineering, medium engineering, and substrate engineering are exploited to improve the enzyme activity and enantioselectivity. With the hydrolysis...

Human milk fat (HMF) triacylglycerols (TAGs) mainly contain palmitic acid esterified at the sn-2 position while oleic and other unsaturated fatty acids are located positions sn-1,3. This study aimed production of HMF substitutes (HMFS) by lipase-catalyzed acidolysis tripalmitin with acid, in a solvent-free medium. Burkholderia cepacia lipase (BCL) was immobilized silica (prepared protic or apro...

aacel9a [β-1,4-endoglucanase, (e.c:3.2.1.4)], was immobilized onto glutaraldehyde activated chitosan macrosphere by covalent attachment. the properties of the immobilized aacel9a were investigated by determining the optimum ph and optimum temperature for activity, thermal stability, and kinetic parameters. the immobilization process shifted the enzyme’s optimum temperature from 65 °c for the fr...

BACKGROUND Industrial-scale biocatalytic synthesis of fine chemicals occurs preferentially as continuous processes employing immobilized enzymes on insoluble porous carriers. Diffusional effects in these systems often create substrate and product concentration gradients between bulk liquid and the carrier. Moreover, some widely-used biotransformation processes induce changes in proton concentra...