Purification and partial characterization of hyaluronate lyase (EC 4.2.2.1) from Propionibacterium acnes

Journal of General Microbiology
E InghamW J Cunliffe

Abstract

Hyaluronidase from Propionibacterium acnes has been purified 13,000-fold from the culture supernatant to homogeneity (as determined by polyacrylamide disc gel electrophoresis). The molecular weight of the purified enzyme was 85,110 as determined by gel filtration. The purified enzyme had a pH optimum at 6.4, was stable between pH 5 and 5.8 and was completely inactivated after 15 min at 50 degrees C. Preliminary studies suggested that the enzyme is active against chondroitin 4- and 6-sulphates, but not against dermatan sulphate. Analysis by paper chromatography of the reaction products from the degradation of hyaluronic acid by bacterial, testicular and P. acnes enzymes suggested that the P. acnes enzyme is similar in its mode of action to other bacterial hyaluronate lyases. The enzyme from P. acnes may thus be tentatively classified as a hyaluronate lyase.

Citations

Aug 31, 2010·BMC Microbiology·Carsten HollandHolger Brüggemann
Apr 1, 1997·Canadian Journal of Microbiology·B SteinerR George
Apr 1, 1986·Applied Biochemistry and Biotechnology·R J LinhardtC L Cooney
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Jan 1, 1984·The British Journal of Dermatology·E InghamW J Cunliffe
Dec 11, 2013·Beneficial Microbes·G J M Christensen, Holger Brüggemann
Feb 15, 2015·Marine Biotechnology·Atsushi KurataNoriaki Kishimoto
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Dec 1, 1981·International Journal of Dermatology·J Greenman

Related Concepts

Ampholytes
Chondroitin Sulfate, Zinc Salt
Dermatan Sulfate
Wydase
Hydrogen-Ion Concentration
Osmolality
Propionibacterium acnes

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