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PubMed · 43744

[Purification and physico-chemical properties of collagenase synthesized by a bacterium of the type Acinetobacter sp].

J C Monboisse·J Labadie·P Gouet
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Abstract

The Acinetobacter spec collagenase has been almost completely purified. This enzyme is a true collagenase the activity of which is high on collagen. The enzyme is active on insoluble collagen, gelatin and the synthetic Pz-peptide, but has no proteolytic activity on casein or bovine serum-albumin. The collagenase was obtained on a simple medium with gelatin and yeast extract. The enzyme was purified by (NH4)2SO4 precipitation. DEAE cellulose column chromatography, Sephadex G 200 gel-filtration. The molecular weight of the enzyme was found to be 102 000 daltons, and its isoelectric point was found to be 7,7 +/- 0,2. The optimum pH and temperature for insoluble collagen hydrolysis were 7.6 and 37 degrees C, respectively; so, this collagenase corresponds to true collagenase. Hydrolysis of Pz-peptide is activated by Ca2+ and inhibited by metal ions (Cu2+, Fe3+, Zn2+, Pb2+, Hg2+). EDTA and o-phenanthroline induced a very significant reduction in enzyme activity. Iodoacetate and p-CMB induced a slight reduction in enzyme activity only at high concentrations (10-2M). The collagenase is most stable for temperatures less than or equal to 50 degrees C.

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AcinetobacterCations, DivalentEdetic AcidEnzyme ActivationHydrogen-Ion ConcentrationIronKineticsMicrobial CollagenaseMolecular WeightPhenanthrolinesEnglish AbstractJournal Article

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J C Monboisse, J Labadie, P Gouet. 1979. [Purification and physico-chemical properties of collagenase synthesized by a bacterium of the type Acinetobacter sp].. https://pubmed.ncbi.nlm.nih.gov/43744/

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