Immobilized enzyme

Although the characteristics of enzymes are extremely unique, their utility in the industry is limited due to the lack of re-usability, stability, and high-cost of production.

[6] For a support material to be ideal, it must be hydrophilic, inert towards enzymes, biocompatible, microbial attack and compression resistant, and must be affordable.

[7][8] Support materials can be organic or inorganic, synthetic or natural (depending on the composition), since they are biomaterial types at the end.

[3][8] As different types of support give different physical and chemical characteristics and properties, which would effect enzyme function, such as: Hydrophilicity/hydrophobicity, surface chemistry, and pore size.

[9] Numerous enzymes of biotechnological importance have been immobilized on various supports (inorganic, organic, composite and nanomaterials) via random multipoint attachment.

However, immobilization via random chemical modification results in a heterogeneous protein population where more than one side chains (amino, carboxyl, thiol etc) present in proteins are linked with the support with potential reduction in activity due to restriction of substrate access to the active site.

[12] In contrast, in site-directed enzyme immobilization, the support can be linked to a single specific amino acid (generally N- or C-termini) in a protein molecule away from the active-site.

These strategies are mainly chemical but may additionally require genetic and enzymatic methods to generate functional groups (that are absent in protein) on the support and enzyme.

Advantages include: In the past, biological washing powders and detergents contained many proteases and lipases that broke down dirt.

In the food industry for example, Immobilized enzymes are used for the manufacturing of several types of zero-calorie sweetners, Allulose for instance is an epimer of fructose, which is different structurally, resulting in it not being absorbable by human bodies when ingested.