The development of methods aimed at increasing enzymes' functional stability in solution, is a subject which is very relevant nowadays, given the multiple applications of these biocatalysts. The strategies previously reported to fulfill this task, are based on the induction of interactions similar to those that contribute to stabilize active enzymes conformation in Nature: covalent intramolecular cross links, hydrogen bridges, increment on the superficial hydrophilicity degree and the formation of electrostatic interactions (ACC 2001 Annual Prize).

This work describes the first reports published in a new area of scientific knowledge: the application of supramolecular chemistry concepts in enzymatic technology. In this sense, the objective of our research has been establishing new procedures led to increase enzymes' functional stability through their supramolecular interaction with cyclodextrin derivatives.

The results presented in this work are different from those which were previously prizewinning in 2001, for their completely novel conception and wider possibilities of practical application. In this result, there are reported four different enzymatic stabilization strategies:

1-The chemical modification of enzymes with monoactive cyclodextrin derivatives.

2-The enzymatic glycosidation of these proteins with oligosaccharide amino derivatives.

3- The covalent conjugation of enzymes with polymeric derivatives of b-cyclodextrin and the use of polymers of b-cyclodextrin as thermoprotective agents of enzymes in aqueous solution. The effectiveness of these procedures is evidenced by the high functional stabilization conferred to the enzymes in study, especially facing processes of thermal and autolytic activation. It is also proven in this work the direct influence of the formation of supramolecular interactions of cyclodextrins-proteins type on stability.