Hyaluronate Lyases and Hyaluronidases

Primary cultures of fibroblasts isolated from embryonic chick skin contain hyaluronidase activity, both associated with the cells and secreted into the medium. The enzyme has a pH optimum at 3.7 and is most active against hyaluronate. The oligosaccharide products of the action of the enzyme on this substrate are similar in size to those from the action of testicular hyaluronidase, ruling out significant degradation by cxo-enzymes. 

The isolation and partial characterization of hyaluronidase which occurs in rat carrageenan granuloma has been reported.  

Culture conditions for inulinase production by an Aspergillus species have been reported. The crystallization and general properties of an extracellular inulinase obtained from an Aspergillus species have been described.  

Studies reported on microbial inulinases include a description of the general properties of extracellular inulinase from a Penicillium species.  

Pseudomonas species isoamylase has been shown to have little action on starch granules. Pseudomonas isoamylase has been shown to hydrolyse (1 6)- 

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