Lysozyme-like enzyme from the scallop Chlamys islandica
A lysozyme-like enzyme isolated from the crystalline style of the scallop Chlamys islandica, was purified by cation exchange chromatography on carboxymethyl cellulose and Mono S columns. The enzyme was optimally active at pH 4.8, similar to that observed for the lysozyme of Mytilis edulis. The prese...
Tallennettuna:
| Päätekijät: | , |
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| Aineistotyyppi: | Online |
| Kieli: | eng |
| Julkaistu: |
Iniversidad Autónoma de Baja California
1992
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| Linkit: | https://www.cienciasmarinas.com.mx/index.php/cmarinas/article/view/881 |
| Tagit: |
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| Yhteenveto: | A lysozyme-like enzyme isolated from the crystalline style of the scallop Chlamys islandica, was purified by cation exchange chromatography on carboxymethyl cellulose and Mono S columns. The enzyme was optimally active at pH 4.8, similar to that observed for the lysozyme of Mytilis edulis. The present enzyme has an unusual 67%, remainder activity at 4ºC when cell walls of Micrococcus lysodeikticus were used as substrate. The enzyme had a specific activity of 486,090 U/mg, corresponding to ten times higher than 1ha1 of hen egg while lysozyme. |
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