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Monika Sellerberg, Diego Di Bartolo, Julia Oberrecht, Jörg Tiller, Peter Walzel
Viscometric measurement of protease activities on gelatine substrate
Appl. Rheol. 24:6 (2014) 62660 (10 pages)
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The knowledge of enzymatic activity is necessary in many industrial processes. The common measurement techniques are
time-consuming and therefore cost-intensive. Measurements of viscosities are a promising approach as a fast and cheap
testing method. The major challenges are to find a suitable substrate with Newtonian flow behavior throughout the whole
testing range as well as a correlation between viscosity of the solution and the decomposed mass. Water based gelatinebuffer-
system as substrate is tested extensively regarding the dependence on different solvents, pH-values and gelatine
batches. All viscosity measurements are performed with a rotational viscometer. It is shown that the gelatine-buffer-system
is independent of the given parameters and found to fulfill the said requirements. A correlation model based on the Martin
equation and necessary assumptions are presented. The required parameters intrinsic viscosity and Martin parameter can be
derived by few measurements with little effort. The digesting enzyme Trypsin is used as model enzyme in the degradation
experiments. The enzyme concentration is varied and the decrease of the viscosity is measured. A dependency between the
enzyme concentration and the enzymatic activity or respectively the viscosity decrease is observed.
► Cite this publication as follows:
Sellerberg M, DiBartolo D, Oberrecht J, Tiller J, Walzel P: Viscometric measurement of protease activities on gelatine substrate, Appl. Rheol. 24 (2014) 62660.
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