THERMAL STABILIZATION OF A CHEMICALLY ORIENTED MODIFIED PULLULANASE

In this article we are interested in stabilized enzymes that hydrolyze macromolecular substrates such as pullulanase with a maximal residual activity after chemical modification in order to obtain a new catalyst that presents a better efficiency compared to stabilized enzymes obtained in previous studies. The efficacity of a stabilized enzyme is defined as the product of the activity times the longevity. The aim of this work is to define the reasons for the low residual activity obtained and to adapt the stabilization method in order to obtain thermostabilized enzyme with a higher activity. We have called this new strategy of stabilization of enzymes chemically oriented modification, as compared to the classical method using a statistical approach.