Ingénierie enzymatique
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Cross Linking

Cross linked enzyme aggregates have emerged as interesting biocatalyst design for immobilization. The new generation enzyme biocatalysts in addition to exhibiting good mechanical stability can be highly active since they do not include large amounts of foreign particulate nonenzymatic material and may have increased stability.
Cross linked enzyme aggregates have emerged as interesting biocatalysts design for immobilization. Precipitation can be used as purification of enzymes.This technique may be implement in a single or reduced operation.

Immobilization of enzymes has been achieved by intermolecular cross-linking of the protein, either to other protein molecules or to functional groups on an insoluble support matrix.. Cross-linking an enzyme to itself is both expensive and insufficient, as some of the protein material will inevitably be acting mainly as a support. This will result in relatively low enzymatic activity. Generally, cross-linking is best used in conjunction with one of the other methods. It is used mostly as a means of stabilizing adsorbed enzymes and also for preventing leakage from polyacrylamide gels.

Related Journals of Cross Linking

Genetic Disorders & Genetic Reports, Hereditary Genetics: Current Research Journals, Gene Technology, Biological Systems : Open Access, Journal of Biotechnology and Biochemistry, The European Journal of Development Research, Food Technology and Biotechnology, Journal of nanobiotechnology, Computational and structural biotechnology journal, Biotechnology and Biochemistry Journal.