User:Shoosh 199/sandbox

This is my sandbox of a Wikipedia article assigned to me (Immobilized enzyme).

The article includes 5 sections varying from immobilized enzyme definition, to methods of immobilization along with other subtitles.

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= Immobilized enzyme (draft) = Enzymes are generally bio-catalysts which play an essential role in the enhancement of chemical reactions in cells without being persistently modified, wasted, nor resulting in the loss of equilibrium of chemical reactions. 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.

An immobilized enzyme is an enzyme, with restricted mobility, attached to an inert, insoluble material—such as calcium alginate (produced by reacting a mixture of sodium alginate solution and enzyme solution with calcium chloride). This can provide increased resistance to changes in conditions such as pH or temperature. It also lets enzymes be held in place throughout the reaction, following which they are easily separated from the products and may be used again - a far more efficient process and so is widely used in industry for enzyme catalysed reactions. An alternative to enzyme immobilization is whole cell immobilization. Immobilized enzymes are easily to be handled, simply separated from their products, and can be reused.

History
The first synthetic immobilized enzyme was made in 1950s, performed by the inclusion of enzyme into polymeric matrices or binding onto carrier substances. Also cross-linking procedure was applied by cross-linking of protein alone or along with the addition of inert materials. Over the last decade various immobilization methods have been developed. Binding the enzyme to previously synthesized carrier materials for example is the mostly preferred method so far. Newly, the procedure of cross-linking of crystals of enzyme is also considered as an exciting substitute. Utilization rate of immobilized enzymes is growing constantly.

Enzyme immobilization methods
Enzymes can be immobilized by physical, or chemical methods being:

Physical adsorption:

 * a straightforward method for reversible immobilization, involving the enzymes being adsorbed or attached physically onto a support substance. Adsorption can take place through weak non-specific forces, such as van der waals, hydrogen bonds, and hydrophobic interactions, whereas in ionic bonding the enzymes are bound through salt linkages.


 * Adsorption on glass, alginate beads or matrix: enzyme is attached to the outside of an inert material. In general, this method is the slowest among those listed here. As adsorption is not a chemical reaction, the active site of the immobilized enzyme may be blocked by the matrix or bead, greatly reducing the activity of the enzyme.

Entrapment:

 * The enzyme is trapped in insoluble beads or microspheres, such as calcium alginate beads. However, these insoluble substances hinder the arrival of the substrate, and the exit of products.

Cross-linking:

 * Cross-linkage: Enzyme molecules are covalently bonded to each other to create a matrix consisting of almost only enzyme. The reaction ensures that the binding site does not cover the enzyme's active site, the activity of the enzyme is only affected by immobility. However, the inflexibility of the covalent bonds precludes the self-healing properties exhibited by chemoadsorbed self-assembled monolayers. Use of a spacer molecule like poly(ethylene glycol) helps reduce the steric hindrance by the substrate in this case.

Covalent bonding:

 * Covalent bond: The enzyme is bound covalently to an insoluble support (such as silica gel or macroporous polymer beads with epoxide groups). This approach provides the strongest enzyme/support interaction, and so the lowest protein leakage during catalysis.

Commercial use
Immobilized enzymes are very important for commercial uses as they possess many benefits to the expenses and processes of the reaction of which include:


 * Convenience: Minuscule amounts of protein dissolve in the reaction, so workup can be much easier. Upon completion, reaction mixtures typically contain only solvent and reaction products.
 * Economy: The immobilized enzyme is easily removed from the reaction making it easy to recycle the biocatalyst. This is particularly useful in processes such as the production of Lactose Free Milk, as the milk can be drained from a container leaving the enzyme (Lactase) inside ready for the next batch.
 * Stability: Immobilized enzymes typically have greater thermal and operational stability than the soluble form of the enzyme.

In the past, biological washing powders and detergents contained many proteases and lipases that broke down dirt. However, when the cleaning products contacted human skin, they created allergic reactions. This is why immobilization of enzymes are important, not just economically.