Characterization of the enzyme complexes produced by two newly isolated thermophylic actinomycete strains during growth on collagen-rich materials
The collagenolytic enzyme complexes secreted by two thermophilic Actinomycetes newly isolated from Bulgarian soils were characterized for their possible application for treating collagen-rich materials. The strains were identified as belonging to genera Microbispora and Thermoactinomyces. The molecu...
Gespeichert in:
| Veröffentlicht in: | Process biochemistry (1991) 2005-04, Vol.40 (5), p.1627-1631 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1631 |
|---|---|
| container_issue | 5 |
| container_start_page | 1627 |
| container_title | Process biochemistry (1991) |
| container_volume | 40 |
| creator | Goshev, I. Gousterova, A. Vasileva-Tonkova, E. Nedkov, P. |
| description | The collagenolytic enzyme complexes secreted by two thermophilic
Actinomycetes newly isolated from Bulgarian soils were characterized for their possible application for treating collagen-rich materials. The strains were identified as belonging to genera
Microbispora and
Thermoactinomyces. The molecular masses of the enzymically active fractions determined by gel chromatography on Sephadex G-100 showed values between 46 and 140
kDa. The enzyme complexes produced by both strains were stable against temperature changes and high ethanol concentrations, which allows effective elimination of different by-products (pigments, nutrient medium components, and metabolites). The comparison with clostridiopeptidase A as well as the inhibitory analysis showed that these enzymes might be considered as “collagenase-like” enzymes. Preliminary experiments showed that a mixture of both enzyme preparations could be applied for pre-treatment of collagen-rich raw materials, e.g., in the pelt industry. |
| doi_str_mv | 10.1016/j.procbio.2004.06.016 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_28503318</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0032959204002420</els_id><sourcerecordid>28503318</sourcerecordid><originalsourceid>FETCH-LOGICAL-c340t-9ede0899a479011a93fe2d44d827d7cdee65169994104cc05c4fa78ecfee29b23</originalsourceid><addsrcrecordid>eNqFUctu2zAQFIoUiOP2EwrwlJtUUtSLpyAw8igQIJfkTNDLlUVDIh2SjqN8Rr64NOx7TrsY7MzO7mTZH0YLRlnzd1vsvIO1cUVJaVXQpkjoj2zBupbnvBTdRep5LfKaMX6ZXYWwpZQzxugi-1oNyiuI6M2nisZZ4noSByRoP-cJCbhpN-IHBpJ26D2gJuuZxIMjFg_jTExwo4oJTRw_ud0wjwZIEjTWTTNgRBKiV8YGovfe2A3ZeHeIA0mbwI2j2qDNvYGBTOpoQo3hV_azTwV_n-sye72_e1k95k_PD_9Wt0858IrGXKBG2gmhqlZQxpTgPZa6qnRXtroFjdjUrBFCVIxWALSGqldth9AjlmJd8mV2fdJNl73tMUQ5mQCYPFl0-yDLrqacsy4N1qdB8C4Ej73ceTMpP0tG5TEBuZXnBOQxAUkbmdDEuznxMF3xbtDLAAZt-qHxCFFqZ75R-A-Pq5dN</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>28503318</pqid></control><display><type>article</type><title>Characterization of the enzyme complexes produced by two newly isolated thermophylic actinomycete strains during growth on collagen-rich materials</title><source>Elsevier ScienceDirect Journals</source><creator>Goshev, I. ; Gousterova, A. ; Vasileva-Tonkova, E. ; Nedkov, P.</creator><creatorcontrib>Goshev, I. ; Gousterova, A. ; Vasileva-Tonkova, E. ; Nedkov, P.</creatorcontrib><description>The collagenolytic enzyme complexes secreted by two thermophilic
Actinomycetes newly isolated from Bulgarian soils were characterized for their possible application for treating collagen-rich materials. The strains were identified as belonging to genera
Microbispora and
Thermoactinomyces. The molecular masses of the enzymically active fractions determined by gel chromatography on Sephadex G-100 showed values between 46 and 140
kDa. The enzyme complexes produced by both strains were stable against temperature changes and high ethanol concentrations, which allows effective elimination of different by-products (pigments, nutrient medium components, and metabolites). The comparison with clostridiopeptidase A as well as the inhibitory analysis showed that these enzymes might be considered as “collagenase-like” enzymes. Preliminary experiments showed that a mixture of both enzyme preparations could be applied for pre-treatment of collagen-rich raw materials, e.g., in the pelt industry.</description><identifier>ISSN: 1359-5113</identifier><identifier>EISSN: 1873-3298</identifier><identifier>DOI: 10.1016/j.procbio.2004.06.016</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>Collagenase activity ; Inhibitors ; Substrate specificity ; Thermophylic Actinomycetes</subject><ispartof>Process biochemistry (1991), 2005-04, Vol.40 (5), p.1627-1631</ispartof><rights>2004 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c340t-9ede0899a479011a93fe2d44d827d7cdee65169994104cc05c4fa78ecfee29b23</citedby><cites>FETCH-LOGICAL-c340t-9ede0899a479011a93fe2d44d827d7cdee65169994104cc05c4fa78ecfee29b23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0032959204002420$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids></links><search><creatorcontrib>Goshev, I.</creatorcontrib><creatorcontrib>Gousterova, A.</creatorcontrib><creatorcontrib>Vasileva-Tonkova, E.</creatorcontrib><creatorcontrib>Nedkov, P.</creatorcontrib><title>Characterization of the enzyme complexes produced by two newly isolated thermophylic actinomycete strains during growth on collagen-rich materials</title><title>Process biochemistry (1991)</title><description>The collagenolytic enzyme complexes secreted by two thermophilic
Actinomycetes newly isolated from Bulgarian soils were characterized for their possible application for treating collagen-rich materials. The strains were identified as belonging to genera
Microbispora and
Thermoactinomyces. The molecular masses of the enzymically active fractions determined by gel chromatography on Sephadex G-100 showed values between 46 and 140
kDa. The enzyme complexes produced by both strains were stable against temperature changes and high ethanol concentrations, which allows effective elimination of different by-products (pigments, nutrient medium components, and metabolites). The comparison with clostridiopeptidase A as well as the inhibitory analysis showed that these enzymes might be considered as “collagenase-like” enzymes. Preliminary experiments showed that a mixture of both enzyme preparations could be applied for pre-treatment of collagen-rich raw materials, e.g., in the pelt industry.</description><subject>Collagenase activity</subject><subject>Inhibitors</subject><subject>Substrate specificity</subject><subject>Thermophylic Actinomycetes</subject><issn>1359-5113</issn><issn>1873-3298</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><recordid>eNqFUctu2zAQFIoUiOP2EwrwlJtUUtSLpyAw8igQIJfkTNDLlUVDIh2SjqN8Rr64NOx7TrsY7MzO7mTZH0YLRlnzd1vsvIO1cUVJaVXQpkjoj2zBupbnvBTdRep5LfKaMX6ZXYWwpZQzxugi-1oNyiuI6M2nisZZ4noSByRoP-cJCbhpN-IHBpJ26D2gJuuZxIMjFg_jTExwo4oJTRw_ud0wjwZIEjTWTTNgRBKiV8YGovfe2A3ZeHeIA0mbwI2j2qDNvYGBTOpoQo3hV_azTwV_n-sye72_e1k95k_PD_9Wt0858IrGXKBG2gmhqlZQxpTgPZa6qnRXtroFjdjUrBFCVIxWALSGqldth9AjlmJd8mV2fdJNl73tMUQ5mQCYPFl0-yDLrqacsy4N1qdB8C4Ej73ceTMpP0tG5TEBuZXnBOQxAUkbmdDEuznxMF3xbtDLAAZt-qHxCFFqZ75R-A-Pq5dN</recordid><startdate>20050401</startdate><enddate>20050401</enddate><creator>Goshev, I.</creator><creator>Gousterova, A.</creator><creator>Vasileva-Tonkova, E.</creator><creator>Nedkov, P.</creator><general>Elsevier Ltd</general><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>F28</scope><scope>FR3</scope></search><sort><creationdate>20050401</creationdate><title>Characterization of the enzyme complexes produced by two newly isolated thermophylic actinomycete strains during growth on collagen-rich materials</title><author>Goshev, I. ; Gousterova, A. ; Vasileva-Tonkova, E. ; Nedkov, P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c340t-9ede0899a479011a93fe2d44d827d7cdee65169994104cc05c4fa78ecfee29b23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Collagenase activity</topic><topic>Inhibitors</topic><topic>Substrate specificity</topic><topic>Thermophylic Actinomycetes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Goshev, I.</creatorcontrib><creatorcontrib>Gousterova, A.</creatorcontrib><creatorcontrib>Vasileva-Tonkova, E.</creatorcontrib><creatorcontrib>Nedkov, P.</creatorcontrib><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><jtitle>Process biochemistry (1991)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Goshev, I.</au><au>Gousterova, A.</au><au>Vasileva-Tonkova, E.</au><au>Nedkov, P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of the enzyme complexes produced by two newly isolated thermophylic actinomycete strains during growth on collagen-rich materials</atitle><jtitle>Process biochemistry (1991)</jtitle><date>2005-04-01</date><risdate>2005</risdate><volume>40</volume><issue>5</issue><spage>1627</spage><epage>1631</epage><pages>1627-1631</pages><issn>1359-5113</issn><eissn>1873-3298</eissn><abstract>The collagenolytic enzyme complexes secreted by two thermophilic
Actinomycetes newly isolated from Bulgarian soils were characterized for their possible application for treating collagen-rich materials. The strains were identified as belonging to genera
Microbispora and
Thermoactinomyces. The molecular masses of the enzymically active fractions determined by gel chromatography on Sephadex G-100 showed values between 46 and 140
kDa. The enzyme complexes produced by both strains were stable against temperature changes and high ethanol concentrations, which allows effective elimination of different by-products (pigments, nutrient medium components, and metabolites). The comparison with clostridiopeptidase A as well as the inhibitory analysis showed that these enzymes might be considered as “collagenase-like” enzymes. Preliminary experiments showed that a mixture of both enzyme preparations could be applied for pre-treatment of collagen-rich raw materials, e.g., in the pelt industry.</abstract><pub>Elsevier Ltd</pub><doi>10.1016/j.procbio.2004.06.016</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1359-5113 |
| ispartof | Process biochemistry (1991), 2005-04, Vol.40 (5), p.1627-1631 |
| issn | 1359-5113 1873-3298 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_28503318 |
| source | Elsevier ScienceDirect Journals |
| subjects | Collagenase activity Inhibitors Substrate specificity Thermophylic Actinomycetes |
| title | Characterization of the enzyme complexes produced by two newly isolated thermophylic actinomycete strains during growth on collagen-rich materials |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-25T10%3A43%3A26IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Characterization%20of%20the%20enzyme%20complexes%20produced%20by%20two%20newly%20isolated%20thermophylic%20actinomycete%20strains%20during%20growth%20on%20collagen-rich%20materials&rft.jtitle=Process%20biochemistry%20(1991)&rft.au=Goshev,%20I.&rft.date=2005-04-01&rft.volume=40&rft.issue=5&rft.spage=1627&rft.epage=1631&rft.pages=1627-1631&rft.issn=1359-5113&rft.eissn=1873-3298&rft_id=info:doi/10.1016/j.procbio.2004.06.016&rft_dat=%3Cproquest_cross%3E28503318%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=28503318&rft_id=info:pmid/&rft_els_id=S0032959204002420&rfr_iscdi=true |