A new method for rapid determination of biocatalyst process stability

In developing enzyme-catalysed processes, a highly active, selective and es pecially stable biocatalyst forms the basis for an economic industrial tech nology. Enzymatic stability is one of the most important properties, but th ere are no good methods for determining it quickly and efficiently. In orde r to solve this problem, a new method for the "accelerated measurement of a ctivity and stability of enzymes (AMASE)" has been developed. Compared to c onventional methods, the new approach differs in two main points. First, th e process of ageing is accelerated by a permanent increase in temperature d uring a continuous experiment, which generates a non-stable response of the enzyme-reactor system. Second, the evaluation procedure is strongly based on a mathematical-mechanistic approach consisting of four steps: assume a d eactivation mechanism, formulate the mathematical model, determine the mode l parameters and finally calculate the biocatalyst characteristics. In this paper, the application of the method for the Lipozyme IM-catalysed hydroly sis of triglycerides in different media is presented.