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${\bf Background}$ Details of the kinetic pathways governing enzymaticcleavage of hyaluronic acid (HA) by hyaluronidase are still widely uncharted.Capillary electrophoresis-based assays were used for accurate quantification ofenzymatic products. A crowding agent was also employed to mimic excluded-volumeconstraints typical of in-vivo conditions.  $ {\bf Scope}$ Introduce a comprehensive kinetic model describing thelate-stage degradation of HA by hyaluronidase and identify the relevant kineticpathways and the associated rates.  ${\bf Major Conclusions}$ All relevant fragmentation and transglycosylationpathways and rates were identified. Two dimers forming a tetramer is thedominant recombination pathway. Macromolecular and self-crowding slow down thekinetics but do not alter the underlying mechanisms.  ${\bf General Significance}$ Our results bring a novel and comprehensivequantitative insight into enzymatic HA degradation. Rationalizing the effect ofcrowding brings the intricate conditions of in-vivo settings a little closer,and also stands as a powerful tool to pinpoint relevant kinetic pathways incomplex systems.

Kinetic theory of Hyaluronan cleavage by Bovine Testicular Hyaluronidase in Standard and Crowded Environments