Production, purification and characterization of novel fibrinolytic enzyme from Bacillus atrophaeus V4
This study was performed to investigate the fibrinolytic enzyme-producing potentials of locally isolated soil bacteria and to purify and characterize the fibrinolytic enzyme of the most potent bacterial isolate. Among 40 isolates, the isolate V4 was found to have the highest potential to produce the...
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| Veröffentlicht in: | Biológia 2023-02, Vol.78 (2), p.591-600 |
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| creator | Varol, Ayse Albayrak, Seyda Ozkan, Hakan Demir, Yeliz Taskin, Mesut Adiguzel, Ahmet |
| description | This study was performed to investigate the fibrinolytic enzyme-producing potentials of locally isolated soil bacteria and to purify and characterize the fibrinolytic enzyme of the most potent bacterial isolate. Among 40 isolates, the isolate V4 was found to have the highest potential to produce the fibrinolytic enzyme. According to 16 S rRNA sequence analysis, the isolate V4 was identified as
Bacillus atrophaeus (
GenBank number: OL662991). The optimal parameters for fibrinolytic enzyme production from
B. atrophaeus
were determined as a skim milk powder concentration of 15 g/L, an initial pH of 7.0, a temperature of 35 °C and an incubation time of 72 h. The molecular weight of the purified enzyme was calculated as 36 kDa. After ammonium sulphate precipitation, ion-exchange chromatography and gel filtration chromotography-based processes, the specific activity of the fibrinolytic enzyme was determined as 6414.7 U/mg. The purified enzyme showed the maximum activity at pH 7.0 and 35 °C. The enzyme was inhibited by PMSF and EDTA. The substrate specifity of the enzyme was in the following order; fibrin (62.3 U/mg) > fibrinogen (46.2 U/mg) > casein (42.1 U/mg) > serum albumin (6.8 U/mg). This is the first report on the fibrinolytic enzyme production potential of the species
B. atrophaeus. |
| doi_str_mv | 10.1007/s11756-022-01281-7 |
| format | Article |
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Bacillus atrophaeus (
GenBank number: OL662991). The optimal parameters for fibrinolytic enzyme production from
B. atrophaeus
were determined as a skim milk powder concentration of 15 g/L, an initial pH of 7.0, a temperature of 35 °C and an incubation time of 72 h. The molecular weight of the purified enzyme was calculated as 36 kDa. After ammonium sulphate precipitation, ion-exchange chromatography and gel filtration chromotography-based processes, the specific activity of the fibrinolytic enzyme was determined as 6414.7 U/mg. The purified enzyme showed the maximum activity at pH 7.0 and 35 °C. The enzyme was inhibited by PMSF and EDTA. The substrate specifity of the enzyme was in the following order; fibrin (62.3 U/mg) > fibrinogen (46.2 U/mg) > casein (42.1 U/mg) > serum albumin (6.8 U/mg). This is the first report on the fibrinolytic enzyme production potential of the species
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Bacillus atrophaeus (
GenBank number: OL662991). The optimal parameters for fibrinolytic enzyme production from
B. atrophaeus
were determined as a skim milk powder concentration of 15 g/L, an initial pH of 7.0, a temperature of 35 °C and an incubation time of 72 h. The molecular weight of the purified enzyme was calculated as 36 kDa. After ammonium sulphate precipitation, ion-exchange chromatography and gel filtration chromotography-based processes, the specific activity of the fibrinolytic enzyme was determined as 6414.7 U/mg. The purified enzyme showed the maximum activity at pH 7.0 and 35 °C. The enzyme was inhibited by PMSF and EDTA. The substrate specifity of the enzyme was in the following order; fibrin (62.3 U/mg) > fibrinogen (46.2 U/mg) > casein (42.1 U/mg) > serum albumin (6.8 U/mg). This is the first report on the fibrinolytic enzyme production potential of the species
B. atrophaeus.</description><subject>Ammonium</subject><subject>Ammonium sulfate</subject><subject>Bacillus atrophaeus</subject><subject>Bacteria</subject><subject>Biomedical and Life Sciences</subject><subject>Casein</subject><subject>Cell Biology</subject><subject>Enzymes</subject><subject>Ethylenediaminetetraacetic acids</subject><subject>Fibrin</subject><subject>Fibrinogen</subject><subject>Gel filtration</subject><subject>Ion exchange</subject><subject>Ion-exchange chromatography</subject><subject>Life Sciences</subject><subject>Microbiology</subject><subject>Molecular weight</subject><subject>Original Article</subject><subject>Parameter identification</subject><subject>Plant Sciences</subject><subject>rRNA</subject><subject>Sequence analysis</subject><subject>Serum albumin</subject><subject>Skim milk</subject><subject>Soil bacteria</subject><subject>Soil microorganisms</subject><subject>Zoology</subject><issn>1336-9563</issn><issn>0006-3088</issn><issn>1336-9563</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNp9UMtOwzAQtBBIlMcPcLLElcD6kTg5QsVLqgQH4Go5jk1dpXGwE6T263EJEpw47ezuzKx2EDojcEkAxFUkRORFBpRmQGhJMrGHZoSxIqvygu3_wYfoKMYVABc5kBmyz8E3ox6c7y5wPwZnnVa7DquuwXqpgtKDCW47Db3Fnf80LbauDq7z7WZwGptuu1kbbINf4xulXduOEash-H6pTIJv_AQdWNVGc_pTj9Hr3e3L_CFbPN0_zq8XmWakGrKcK0Z4WSujTV0oKrjlFa9pzU0OvBZFCYRraksQBVTKpEXZlPnuG2WhbNgxOp98--A_RhMHufJj6NJJSZNaMICqSiw6sXTwMQZjZR_cWoWNJCB3ecopT5nylN95SpFEbBLFRO7eTfi1_kf1BdeteYk</recordid><startdate>20230201</startdate><enddate>20230201</enddate><creator>Varol, Ayse</creator><creator>Albayrak, Seyda</creator><creator>Ozkan, Hakan</creator><creator>Demir, Yeliz</creator><creator>Taskin, Mesut</creator><creator>Adiguzel, Ahmet</creator><general>Springer International Publishing</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><orcidid>https://orcid.org/0000-0001-8848-6647</orcidid></search><sort><creationdate>20230201</creationdate><title>Production, purification and characterization of novel fibrinolytic enzyme from Bacillus atrophaeus V4</title><author>Varol, Ayse ; 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Among 40 isolates, the isolate V4 was found to have the highest potential to produce the fibrinolytic enzyme. According to 16 S rRNA sequence analysis, the isolate V4 was identified as
Bacillus atrophaeus (
GenBank number: OL662991). The optimal parameters for fibrinolytic enzyme production from
B. atrophaeus
were determined as a skim milk powder concentration of 15 g/L, an initial pH of 7.0, a temperature of 35 °C and an incubation time of 72 h. The molecular weight of the purified enzyme was calculated as 36 kDa. After ammonium sulphate precipitation, ion-exchange chromatography and gel filtration chromotography-based processes, the specific activity of the fibrinolytic enzyme was determined as 6414.7 U/mg. The purified enzyme showed the maximum activity at pH 7.0 and 35 °C. The enzyme was inhibited by PMSF and EDTA. The substrate specifity of the enzyme was in the following order; fibrin (62.3 U/mg) > fibrinogen (46.2 U/mg) > casein (42.1 U/mg) > serum albumin (6.8 U/mg). This is the first report on the fibrinolytic enzyme production potential of the species
B. atrophaeus.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><doi>10.1007/s11756-022-01281-7</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0001-8848-6647</orcidid></addata></record> |
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| subjects | Ammonium Ammonium sulfate Bacillus atrophaeus Bacteria Biomedical and Life Sciences Casein Cell Biology Enzymes Ethylenediaminetetraacetic acids Fibrin Fibrinogen Gel filtration Ion exchange Ion-exchange chromatography Life Sciences Microbiology Molecular weight Original Article Parameter identification Plant Sciences rRNA Sequence analysis Serum albumin Skim milk Soil bacteria Soil microorganisms Zoology |
| title | Production, purification and characterization of novel fibrinolytic enzyme from Bacillus atrophaeus V4 |
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