A New Method for Rapid Determination of Biocatalyst Process Stability

Abstract

In developing enzyme-catalysed processes, a highly active, selective and especially stable biocatalyst forms the basis for an economic industrial technology. Enzymatic stability is one of the most important properties, but there are no good methods for determining it quickly and efficiently. In order to solve this problem, a new method for the “accelerated measurement of activity and stability of enzymes (AMASE)” has been developed. Compared to conventional methods, the new approach differs in two main points. First, the process of ageing is accelerated by a permanent increase in temperature during 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 deactivation mechanism, formulate the mathematical model, determine the model parameters and finally calculate the biocatalyst characteristics. In this paper, the application of the method for the Lipozyme IM-catalysed hydrolysis of triglycerides in different media is presented.

Key Words:

• Enzyme deactivation
• Deactivation mechanisms
• In situ characterisation
• Process development
• Initial activity
• Half-life time