Understanding enzyme immobilisation

Abstract

Enzymes are versatile catalysts in the laboratory and on an industrial scale. To broaden their applicability in the laboratory and to ensure their (re)use in manufacturing the stability of enzymes can often require improvement. Immobilisation can address the issue of enzymatic instability. Immobilisation can also help to enable the employment of enzymes in different solvents, at extremes of pH and temperature and exceptionally high substrate concentrations. At the same time substrate-specificity, enantioselectivity and reactivity can be modified. However, most often the molecular and physical-chemical bases of these phenomena have not been elucidated yet. This tutorial review focuses on the understanding of enzyme immobilisation.

Immobilisation of laccase on Eupergit supports and its application for the removal of endocrine disrupting chemicals in a packed-bed reactor

“…Moreover, the formation of multiple covalent bonds between the enzyme and the support reduces conformational flexibility and thermal vibrations, thus preventing protein unfolding and denaturation (Hanefeld et al 2009). The application of covalent immobilisation techniques considers two different possibilities: either the use of inert carriers which can be properly activated or even the use of active supports commercially available.…”

Substrate-dependent kinetics in tyrosinase-based biosensing: amperometry vs. spectrophotometry

“…Although immobilized tyrosinase on the electrode surface has been reported to result in increased enzyme stability and allows reusing the sensor for a few times [22], in several cases it introduces problems with mass transfer of the substrate to the enzyme [23]. A much simpler approach is to add free enzyme to the sample solution as suggested in the recent publication of Adamski et al [24].…”

Lipase-Catalyzed Kinetic Resolution of 1-(2-Hydroxycyclohexyl)Indoles in Batch and Continuous-Flow Systems

“…[46][47][48][49][50][51] Selectivity, specificity, catalytic activity and enzyme stability are key factors affecting the efficiency of biocatalysts. [16][17][18][20][21][22][23][24][25][26] Immobilization can often improve these key properties [46][47][48][49][50][51] and also enabling the use of biocatalysts under continuous-flow conditions. 19 Among the factors influencing selectivity, catalytic activity and stability of the biocatalysts under continuous-flow conditions, temperature effects are the most important.…”