Biochemical and bacteriological properties of the lysozyme of the clam Tivela stultorum
A lysozyme-like enzyme from the crystalline style of the clam Tivela stultorum was purified by chromatography of cationic exchange in carboxymethyl cellulose. The product had a specific activity of 25,407 units per milligram of protein, which represents a purification of 100 times. The spe...
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Iniversidad Autónoma de Baja California
2000
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oai:cienciasmarinas.com.mx:article-5812019-05-08T19:36:57Z Biochemical and bacteriological properties of the lysozyme of the clam Tivela stultorum Propiedades bioquímicas y bacteriológicas de la lisozima de la almeja Tivela stultorum Montenegro-Ortega, RE Viana, MT marine enzymes lysozyme bacteriological characterization enzimas marinas lisozima bacteriológicas caracterización A lysozyme-like enzyme from the crystalline style of the clam Tivela stultorum was purified by chromatography of cationic exchange in carboxymethyl cellulose. The product had a specific activity of 25,407 units per milligram of protein, which represents a purification of 100 times. The specific activity observed with this enzyme was almost six times greater than the activity observed in the hen egg-white lysozyme under the same conditions. Using the isoelectric focusing technique, a component was observed that indicates an isoelectric point of 7.7 (IEF-PAGE, Phast Gel). A one-dimensional electrophoresis (SDS-PAGE) revealed an apparent molecular weight of 17,000 daltons. The enzyme was optimally active at pH 5.6–5.8, in 0.1 M phosphate-citrate buffer, with maximum activity at a temperature of 40ºC, and an ionic strength of 0.1043. At 4ºC, the lysozyme presented 26.7% of remnant activity, and was highly stable at elevated temperatures (90ºC) and extreme pHs, from 2.8 to 11.8, with activities above 75%. This enzyme proved to have antimicrobial properties with or without EDTA in the lysis of three bacteria (Streptococcus alfa, Micrococcus lisodeikticus and Escherichia coli), whereas hen egg lysozyme showed lysis in the presence of EDTA on S. alfa and E. coli. The results were also compared against the lysozyme of the scallop Chlamys islandica. Una enzima tipo lisozima proveniente del estilete cristalino de la almeja Tivela stultorum fue purificada por cromatografía de intercambio catiónico en carboximetil celulosa. El producto tuvo una actividad específica de 25,407 unidades por miligramo de proteína, representando una purificación de 100 veces. La actividad específica observada por esta enzima fue casi seis veces mayor que la actividad observada en la lisozima de clara de huevo de gallina bajo las mismas condiciones. Mediante la técnica de isoelectroenfoque se observó un componente indicando un punto isoeléctrico de 7.7 (IEF-PAGE, Phast Gel). Por medio de electroforesis de una dimensión (SDS-PAGE), se sugiere un peso molecular aparente de 17,000 daltons. La enzima fue óptimamente activa a pH de 5.6 a 5.8, en amortiguador citrato fosfato 0.1 M, con actividad máxima a una temperatura de 40ºC, y con una fuerza iónica de 0.1043. A 4ºC la lisozima presentó 26.7% de actividad remanente, además de mostrar ser altamente estable a temperatures elevadas (90ºC) y pHs extremos con actividades por arriba del 75%, en un rango de pHs de 2.8 a 11.8. Dicha enzima mostró tener propiedades antimicrobianas en presencia y ausencia de EDTA sobre la lisis de tres bacterias (Streptococcus alfa, Micrococcus lisodeikticus y Escherichia coli), mientras que la lisozima de huevo de gallina sólo mostró lisis en presencia de EDTA sobre S. alfa y E. coli. Los resultados también fueron comparados contra una lisozima de la almeja ártica Chlamys islandica. Iniversidad Autónoma de Baja California 2000-03-06 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion Peer-reviewed Article Artículo Arbitrado application/pdf https://www.cienciasmarinas.com.mx/index.php/cmarinas/article/view/581 10.7773/cm.v26i2.581 Ciencias Marinas; Vol. 26 No. 2 (2000); 225-251 Ciencias Marinas; Vol. 26 Núm. 2 (2000); 225-251 2395-9053 0185-3880 eng https://www.cienciasmarinas.com.mx/index.php/cmarinas/article/view/581/518 |
| institution |
Ciencias Marinas |
| collection |
OJS |
| language |
eng |
| format |
Online |
| author |
Montenegro-Ortega, RE Viana, MT |
| spellingShingle |
Montenegro-Ortega, RE Viana, MT Biochemical and bacteriological properties of the lysozyme of the clam Tivela stultorum |
| author_facet |
Montenegro-Ortega, RE Viana, MT |
| author_sort |
Montenegro-Ortega, RE |
| title |
Biochemical and bacteriological properties of the lysozyme of the clam Tivela stultorum |
| title_short |
Biochemical and bacteriological properties of the lysozyme of the clam Tivela stultorum |
| title_full |
Biochemical and bacteriological properties of the lysozyme of the clam Tivela stultorum |
| title_fullStr |
Biochemical and bacteriological properties of the lysozyme of the clam Tivela stultorum |
| title_full_unstemmed |
Biochemical and bacteriological properties of the lysozyme of the clam Tivela stultorum |
| title_sort |
biochemical and bacteriological properties of the lysozyme of the clam tivela stultorum |
| description |
A lysozyme-like enzyme from the crystalline style of the clam Tivela stultorum was purified by chromatography of cationic exchange in carboxymethyl cellulose. The product had a specific activity of 25,407 units per milligram of protein, which represents a purification of 100 times. The specific activity observed with this enzyme was almost six times greater than the activity observed in the hen egg-white lysozyme under the same conditions. Using the isoelectric focusing technique, a component was observed that indicates an isoelectric point of 7.7 (IEF-PAGE, Phast Gel). A one-dimensional electrophoresis (SDS-PAGE) revealed an apparent molecular weight of 17,000 daltons. The enzyme was optimally active at pH 5.6–5.8, in 0.1 M phosphate-citrate buffer, with maximum activity at a temperature of 40ºC, and an ionic strength of 0.1043. At 4ºC, the lysozyme presented 26.7% of remnant activity, and was highly stable at elevated temperatures (90ºC) and extreme pHs, from 2.8 to 11.8, with activities above 75%. This enzyme proved to have antimicrobial properties with or without EDTA in the lysis of three bacteria (Streptococcus alfa, Micrococcus lisodeikticus and Escherichia coli), whereas hen egg lysozyme showed lysis in the presence of EDTA on S. alfa and E. coli. The results were also compared against the lysozyme of the scallop Chlamys islandica. |
| publisher |
Iniversidad Autónoma de Baja California |
| publishDate |
2000 |
| url |
https://www.cienciasmarinas.com.mx/index.php/cmarinas/article/view/581 |
| _version_ |
1715723985962926080 |
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