Immobilized Biomaterials—Techniques and Applications

Abstract

The immobilization of enzymes, cofactors and whole cells offers the potential of economical exploitation of biomaterial activity. Enzymes or cells can be immobilized by binding to carriers through adsorption or covalent linkages or by entrapment in a polymer matrix or microencapsulation. The development of immobilized biomaterial systems requires the involvement of biochemical, kinetics and reactor design principles. Examples of commercial scale applications of immobilized biomaterial systems are the production of a fructose-rich syrup from starch and the synthesis of L-amino acids by selective hydrolysis of N-acyl-D,Lamino acids.

Metal-Enzyme Frameworks: Role of Metal Ions in Promoting Enzyme Self-Assembly on α-Zirconium(IV) Phosphate Nanoplates

“…Protein self-assembly is challenging because of the large size of proteins, multiple functional groups on their surfaces, their fragility to solvents, sensitivity to particular ions and extreme pH, and their vulnerability to degradation by proteases, which are ubiquitous. Protein assemblies are increasingly being used in biosensing, biomaterials, biocatalysis, and biomedicine . Therefore, it is critical to understand how such assemblies can be constructed by a systematic approach and establish the details of the mechanism of protein assembly, so that protein assembly can be controlled in a rational, predictable manner.…”

Protein Patterning with a Photoactivatable Derivative of Biotin

“…Turning to the immobilization chemistry itself there are numerous reagents available for covalently crosslinking proteins to the modified surface (Sharma et al, 1982); however, arguably the mildest and most generic approach is to use biotin-avidin complexes (Wilchek and Bayer, 1988). There are many advantages in using the avidin-biotin system for protein immobilization; for example, the complex that is formed has an extremely high affinity (K a ) 10 15 M -1 ) (Green, 1975).…”