Biocatalyst Immobilization and Modification

es protein engineering, chemical approaches including chemical modification and immobilization are employed in designing biocatalysts with desirable bio-properties for industrial applications. Enzyme immobilization, first commercialized in the 1960s, has been well developed to facilitate the reusability and recovery of enzymes. High stabilization of a biocatalyst, such as pH and thermal stability, can often be achieved through immobilization, and enhanced activities are demonstrated in an increasing number of recent reports.
Immobilization can be generally categorized into carrier-bound immobilization and carrier-free immobilization. In carrier-bound applications, solid support attachment is a typical example, where enzymes are attached in solid surfaces either through physical adsorption or covalent linkages. Entrapment and cross-linking are other alternative methods in this category. In carrier-free applications, cross-linked enzyme aggregates (CLEAs) are developed by simple precipitation of the enzyme from a solution by adding salt, (such as ammonium sulfate), or a water-miscible organic solvent, followed by cross-linking with a bifunctional reagent. This method has been demonstrated to be sufficient for two or more enzymes and known as combi-CLEA.
Creative Enzymes provide the best biocatalyst immobilization and modification services for researchers. With years of experience in this field, we offer professional one-stop services with reliable outcomes, improved performance, and biophysical analysis:
Custom biocatalyst immobilization design;
Process optimization;
Activity and stability measurements;
Process scaling-up.