Production and properties of thermostable proteases from bacillus thermoleovorans strain HSR
The thermophilic bacterium Bacillus thermoleovorans strain HSR secretes thermostable extracellular proteases when cultivated in the presence of tryptone. The proteases which are found to be of the metallo-protease type, showed maximal activity when incubated at 80°C and pH 7.0. The enzymes are therm...
Saved in:
| Main Author: | |
|---|---|
| Other Authors: | , |
| Format: | article |
| Published: |
2000
|
| Online Access: | http://hdl.handle.net/10725/5110 http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php http://lsj.cnrs.edu.lb/wp-content/uploads/2016/01/hashwa.pdf |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1864513465042862080 |
|---|---|
| author | Tokajian, Sima |
| author2 | Hashwa, Fuad Sunna, Anwar |
| author2_role | author author |
| author_facet | Tokajian, Sima Hashwa, Fuad Sunna, Anwar |
| author_role | author |
| dc.creator.none.fl_str_mv | Tokajian, Sima Hashwa, Fuad Sunna, Anwar |
| dc.date.none.fl_str_mv | 2000 2017-01-30T10:08:33Z 2017-01-30T10:08:33Z 2017-01-30 |
| dc.identifier.none.fl_str_mv | 1561-3410 http://hdl.handle.net/10725/5110 Tokajian, S., Sunna, A., & Hashwa, F. (2000). PRODUCTION AND PROPERTIES OF THERMOSTABLE PROTEASES FROM BACILLUS THERMOLEOVORANS STRAIN HSR. Journal Scientifique Libanais, 1(1), 49. http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php http://lsj.cnrs.edu.lb/wp-content/uploads/2016/01/hashwa.pdf |
| dc.language.none.fl_str_mv | en |
| dc.relation.none.fl_str_mv | Journal Scientifique Libanais |
| dc.rights.*.fl_str_mv | info:eu-repo/semantics/openAccess |
| dc.title.none.fl_str_mv | Production and properties of thermostable proteases from bacillus thermoleovorans strain HSR |
| dc.type.none.fl_str_mv | Article info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/article |
| description | The thermophilic bacterium Bacillus thermoleovorans strain HSR secretes thermostable extracellular proteases when cultivated in the presence of tryptone. The proteases which are found to be of the metallo-protease type, showed maximal activity when incubated at 80°C and pH 7.0. The enzymes are thermostable at temperatures between 60 and 80°C in the absence of substrate. Calcium is not required for thermostability. Cu2+, Hg2+ and EDTA inhibit the protease activity while Fe2+ and Fe3+ ions enhanced the activity. SDS-PAGE studies indicate the presence of multiple protease activity bands with molecular masses between 40 and 57 kDa. The proteases show higher activity towards short synthetic peptides while a decrease in specificity was observed with longer peptides. |
| eu_rights_str_mv | openAccess |
| format | article |
| id | LAURepo_757bb09a53a35ff3908b2dd1eb181de8 |
| identifier_str_mv | 1561-3410 Tokajian, S., Sunna, A., & Hashwa, F. (2000). PRODUCTION AND PROPERTIES OF THERMOSTABLE PROTEASES FROM BACILLUS THERMOLEOVORANS STRAIN HSR. Journal Scientifique Libanais, 1(1), 49. |
| language_invalid_str_mv | en |
| network_acronym_str | LAURepo |
| network_name_str | Lebanese American University repository |
| oai_identifier_str | oai:laur.lau.edu.lb:10725/5110 |
| publishDate | 2000 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| spelling | Production and properties of thermostable proteases from bacillus thermoleovorans strain HSRTokajian, SimaHashwa, FuadSunna, AnwarThe thermophilic bacterium Bacillus thermoleovorans strain HSR secretes thermostable extracellular proteases when cultivated in the presence of tryptone. The proteases which are found to be of the metallo-protease type, showed maximal activity when incubated at 80°C and pH 7.0. The enzymes are thermostable at temperatures between 60 and 80°C in the absence of substrate. Calcium is not required for thermostability. Cu2+, Hg2+ and EDTA inhibit the protease activity while Fe2+ and Fe3+ ions enhanced the activity. SDS-PAGE studies indicate the presence of multiple protease activity bands with molecular masses between 40 and 57 kDa. The proteases show higher activity towards short synthetic peptides while a decrease in specificity was observed with longer peptides.PublishedN/A2017-01-30T10:08:33Z2017-01-30T10:08:33Z20002017-01-30Articleinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article1561-3410http://hdl.handle.net/10725/5110Tokajian, S., Sunna, A., & Hashwa, F. (2000). PRODUCTION AND PROPERTIES OF THERMOSTABLE PROTEASES FROM BACILLUS THERMOLEOVORANS STRAIN HSR. Journal Scientifique Libanais, 1(1), 49.http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.phphttp://lsj.cnrs.edu.lb/wp-content/uploads/2016/01/hashwa.pdfenJournal Scientifique Libanaisinfo:eu-repo/semantics/openAccessoai:laur.lau.edu.lb:10725/51102021-03-19T10:00:48Z |
| spellingShingle | Production and properties of thermostable proteases from bacillus thermoleovorans strain HSR Tokajian, Sima |
| status_str | publishedVersion |
| title | Production and properties of thermostable proteases from bacillus thermoleovorans strain HSR |
| title_full | Production and properties of thermostable proteases from bacillus thermoleovorans strain HSR |
| title_fullStr | Production and properties of thermostable proteases from bacillus thermoleovorans strain HSR |
| title_full_unstemmed | Production and properties of thermostable proteases from bacillus thermoleovorans strain HSR |
| title_short | Production and properties of thermostable proteases from bacillus thermoleovorans strain HSR |
| title_sort | Production and properties of thermostable proteases from bacillus thermoleovorans strain HSR |
| url | http://hdl.handle.net/10725/5110 http://libraries.lau.edu.lb/research/laur/terms-of-use/articles.php http://lsj.cnrs.edu.lb/wp-content/uploads/2016/01/hashwa.pdf |