Purification and Characterization of Keratinase from Bacillus licheniformis dcs1 for Poultry Waste Processing
Feather wastes-byproduct of commercial poultry processing plant is produced in large amounts. Keratinolytic enzymes produced by feather degrading bacteria can easily degrade these waste products releasing pure keratin as a residue. The aim of present study was to isolate, and characterize feather de...
Gespeichert in:
| Veröffentlicht in: | Journal of Oleo Science 2022, Vol.71(5), pp.693-700 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 700 |
|---|---|
| container_issue | 5 |
| container_start_page | 693 |
| container_title | Journal of Oleo Science |
| container_volume | 71 |
| creator | Liaqat, Iram Ali, Sikander Butt, Abida Durrani, Arjumand Iqbal Zafar, Urooj Saleem, Sadiah Naseem, Sajida Ahsan, Fatima |
| description | Feather wastes-byproduct of commercial poultry processing plant is produced in large amounts. Keratinolytic enzymes produced by feather degrading bacteria can easily degrade these waste products releasing pure keratin as a residue. The aim of present study was to isolate, and characterize feather degrading bacteria as well as assess the keratinolytic potential of purified enzyme. Three feather degrading bacteria (dps3, wps1 and dcs1) were isolated from feathers of domestic chickens. Preliminary characterization of isolated bacteria revealed these isolates belonging to genus Bacillus. 16S rRNA gene sequencing identified the isolates as B. subtilis dps3 (MW255302), B. cereus wps1 (MW255303) and B. licheniformis dcs1 (MW255304). Cell free supernatant of B. licheniformis dcs1 degraded feathers completely in 14 days indicating its keratinolytic ability. Purification of keratinase enzyme from B. licheniformis dcs1 was performed using column chromatography. SDS-PAGE indicated its molecular weight as 32 KDa. Kerotinolytice activity was maximum at optimum pH of 7 and 45℃ temperature. Enzyme showed the potential to degrade keratin material such as hairs and nails of humans. Findings of current study suggested that purified enzyme possess potential to upgrade nutritional quality of poultry waste containing keratin and might play as important biotechnological tool for keratin hydrolysis. |
| doi_str_mv | 10.5650/jos.ess21426 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_2658286037</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2658286037</sourcerecordid><originalsourceid>FETCH-LOGICAL-c630t-29fd427b4bfac796ce78430a9d1d15d0687704127f5638fbf2a9129028de93583</originalsourceid><addsrcrecordid>eNpFUcFu3CAQtapWTZr21nOF1GudDmAMHJtVk1aNlD2k6hGxGBIsDCnYh_Trw8bZ7YUZzTzee3rTNB8xnLOewdcxlXNbCsEd6V81p5h2vKWUkdfPPWuFZPykeVfKCFDnjL9tTiijgkssTptpu2TvvNGzTxHpOKDNvc7azDb7f-swOfTL5tpHXSxyOU3oQhsfwlJQ8ObeRu9SnnxBgykY1R5t0xLm_Ij-6DJbtM3JVIc-3r1v3jgdiv3wUs-a35ffbzc_2uubq5-bb9et6SnMLZFu6AjfdTunDZe9sVx0FLQc8IDZAL3gHDpMuGM9FW7niJaYSCBisJIyQc-azyvvQ05_F1tmNaYlxyqpSM8EET1QXlFfVpTJqZRsnXrIftL5UWFQ-2zrr6IO2Vb4pxfSZTfZ4Qg-hFkBVyugbmuiIcXgo_0vPYw8BVspCRCiADgGti8KekkVcIAOMHSdrEwXK9NYZn1nj1I6z94E--yLY8X2z8HfcWnqAZWN9AmbdKUy</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2658286037</pqid></control><display><type>article</type><title>Purification and Characterization of Keratinase from Bacillus licheniformis dcs1 for Poultry Waste Processing</title><source>J-STAGE (Free - Japanese)</source><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>Free Full-Text Journals in Chemistry</source><source>EZB*</source><creator>Liaqat, Iram ; Ali, Sikander ; Butt, Abida ; Durrani, Arjumand Iqbal ; Zafar, Urooj ; Saleem, Sadiah ; Naseem, Sajida ; Ahsan, Fatima</creator><creatorcontrib>Liaqat, Iram ; Ali, Sikander ; Butt, Abida ; Durrani, Arjumand Iqbal ; Zafar, Urooj ; Saleem, Sadiah ; Naseem, Sajida ; Ahsan, Fatima ; Microbiology Lab ; University of Veterinary and Animal Sciences ; University of the Punjab ; Department of Chemistry ; Department of Zoology ; Institute of Industrial Biotechnology ; University of Engineering and Technology ; Department of Microbiology ; Division of Science and Technology ; University of Education ; University of Karachi ; Government College University</creatorcontrib><description>Feather wastes-byproduct of commercial poultry processing plant is produced in large amounts. Keratinolytic enzymes produced by feather degrading bacteria can easily degrade these waste products releasing pure keratin as a residue. The aim of present study was to isolate, and characterize feather degrading bacteria as well as assess the keratinolytic potential of purified enzyme. Three feather degrading bacteria (dps3, wps1 and dcs1) were isolated from feathers of domestic chickens. Preliminary characterization of isolated bacteria revealed these isolates belonging to genus Bacillus. 16S rRNA gene sequencing identified the isolates as B. subtilis dps3 (MW255302), B. cereus wps1 (MW255303) and B. licheniformis dcs1 (MW255304). Cell free supernatant of B. licheniformis dcs1 degraded feathers completely in 14 days indicating its keratinolytic ability. Purification of keratinase enzyme from B. licheniformis dcs1 was performed using column chromatography. SDS-PAGE indicated its molecular weight as 32 KDa. Kerotinolytice activity was maximum at optimum pH of 7 and 45℃ temperature. Enzyme showed the potential to degrade keratin material such as hairs and nails of humans. Findings of current study suggested that purified enzyme possess potential to upgrade nutritional quality of poultry waste containing keratin and might play as important biotechnological tool for keratin hydrolysis.</description><identifier>ISSN: 1345-8957</identifier><identifier>EISSN: 1347-3352</identifier><identifier>DOI: 10.5650/jos.ess21426</identifier><identifier>PMID: 35387918</identifier><language>eng</language><publisher>Japan: Japan Oil Chemists' Society</publisher><subject>Animals ; B. licheniformis ; Bacillus licheniformis - metabolism ; Bacteria ; Chickens - genetics ; Chickens - metabolism ; Column chromatography ; Degradation ; Enzymes ; feather degrading bacteria ; Feathers ; Gene sequencing ; Hydrogen-Ion Concentration ; Keratin ; keratinolytic enzymes ; Keratins - analysis ; Keratins - metabolism ; Peptide Hydrolases - chemistry ; Peptide Hydrolases - genetics ; Peptide Hydrolases - metabolism ; Poultry ; Poultry - genetics ; Poultry - metabolism ; poultry wastes ; Purification ; RNA, Ribosomal, 16S ; Temperature ; Waste disposal</subject><ispartof>Journal of Oleo Science, 2022, Vol.71(5), pp.693-700</ispartof><rights>2022 by Japan Oil Chemists' Society</rights><rights>2022. This work is published under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c630t-29fd427b4bfac796ce78430a9d1d15d0687704127f5638fbf2a9129028de93583</citedby><cites>FETCH-LOGICAL-c630t-29fd427b4bfac796ce78430a9d1d15d0687704127f5638fbf2a9129028de93583</cites><orcidid>0000-0002-9211-2944 ; 0000-0001-6506-1080 ; 0000-0001-7098-8649 ; 0000-0002-5218-6471 ; 0000-0002-4638-8253 ; 0000-0002-3754-3135 ; 0000-0002-3909-9242</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,864,1883,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35387918$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liaqat, Iram</creatorcontrib><creatorcontrib>Ali, Sikander</creatorcontrib><creatorcontrib>Butt, Abida</creatorcontrib><creatorcontrib>Durrani, Arjumand Iqbal</creatorcontrib><creatorcontrib>Zafar, Urooj</creatorcontrib><creatorcontrib>Saleem, Sadiah</creatorcontrib><creatorcontrib>Naseem, Sajida</creatorcontrib><creatorcontrib>Ahsan, Fatima</creatorcontrib><creatorcontrib>Microbiology Lab</creatorcontrib><creatorcontrib>University of Veterinary and Animal Sciences</creatorcontrib><creatorcontrib>University of the Punjab</creatorcontrib><creatorcontrib>Department of Chemistry</creatorcontrib><creatorcontrib>Department of Zoology</creatorcontrib><creatorcontrib>Institute of Industrial Biotechnology</creatorcontrib><creatorcontrib>University of Engineering and Technology</creatorcontrib><creatorcontrib>Department of Microbiology</creatorcontrib><creatorcontrib>Division of Science and Technology</creatorcontrib><creatorcontrib>University of Education</creatorcontrib><creatorcontrib>University of Karachi</creatorcontrib><creatorcontrib>Government College University</creatorcontrib><title>Purification and Characterization of Keratinase from Bacillus licheniformis dcs1 for Poultry Waste Processing</title><title>Journal of Oleo Science</title><addtitle>J Oleo Sci</addtitle><description>Feather wastes-byproduct of commercial poultry processing plant is produced in large amounts. Keratinolytic enzymes produced by feather degrading bacteria can easily degrade these waste products releasing pure keratin as a residue. The aim of present study was to isolate, and characterize feather degrading bacteria as well as assess the keratinolytic potential of purified enzyme. Three feather degrading bacteria (dps3, wps1 and dcs1) were isolated from feathers of domestic chickens. Preliminary characterization of isolated bacteria revealed these isolates belonging to genus Bacillus. 16S rRNA gene sequencing identified the isolates as B. subtilis dps3 (MW255302), B. cereus wps1 (MW255303) and B. licheniformis dcs1 (MW255304). Cell free supernatant of B. licheniformis dcs1 degraded feathers completely in 14 days indicating its keratinolytic ability. Purification of keratinase enzyme from B. licheniformis dcs1 was performed using column chromatography. SDS-PAGE indicated its molecular weight as 32 KDa. Kerotinolytice activity was maximum at optimum pH of 7 and 45℃ temperature. Enzyme showed the potential to degrade keratin material such as hairs and nails of humans. Findings of current study suggested that purified enzyme possess potential to upgrade nutritional quality of poultry waste containing keratin and might play as important biotechnological tool for keratin hydrolysis.</description><subject>Animals</subject><subject>B. licheniformis</subject><subject>Bacillus licheniformis - metabolism</subject><subject>Bacteria</subject><subject>Chickens - genetics</subject><subject>Chickens - metabolism</subject><subject>Column chromatography</subject><subject>Degradation</subject><subject>Enzymes</subject><subject>feather degrading bacteria</subject><subject>Feathers</subject><subject>Gene sequencing</subject><subject>Hydrogen-Ion Concentration</subject><subject>Keratin</subject><subject>keratinolytic enzymes</subject><subject>Keratins - analysis</subject><subject>Keratins - metabolism</subject><subject>Peptide Hydrolases - chemistry</subject><subject>Peptide Hydrolases - genetics</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Poultry</subject><subject>Poultry - genetics</subject><subject>Poultry - metabolism</subject><subject>poultry wastes</subject><subject>Purification</subject><subject>RNA, Ribosomal, 16S</subject><subject>Temperature</subject><subject>Waste disposal</subject><issn>1345-8957</issn><issn>1347-3352</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFUcFu3CAQtapWTZr21nOF1GudDmAMHJtVk1aNlD2k6hGxGBIsDCnYh_Trw8bZ7YUZzTzee3rTNB8xnLOewdcxlXNbCsEd6V81p5h2vKWUkdfPPWuFZPykeVfKCFDnjL9tTiijgkssTptpu2TvvNGzTxHpOKDNvc7azDb7f-swOfTL5tpHXSxyOU3oQhsfwlJQ8ObeRu9SnnxBgykY1R5t0xLm_Ij-6DJbtM3JVIc-3r1v3jgdiv3wUs-a35ffbzc_2uubq5-bb9et6SnMLZFu6AjfdTunDZe9sVx0FLQc8IDZAL3gHDpMuGM9FW7niJaYSCBisJIyQc-azyvvQ05_F1tmNaYlxyqpSM8EET1QXlFfVpTJqZRsnXrIftL5UWFQ-2zrr6IO2Vb4pxfSZTfZ4Qg-hFkBVyugbmuiIcXgo_0vPYw8BVspCRCiADgGti8KekkVcIAOMHSdrEwXK9NYZn1nj1I6z94E--yLY8X2z8HfcWnqAZWN9AmbdKUy</recordid><startdate>20220101</startdate><enddate>20220101</enddate><creator>Liaqat, Iram</creator><creator>Ali, Sikander</creator><creator>Butt, Abida</creator><creator>Durrani, Arjumand Iqbal</creator><creator>Zafar, Urooj</creator><creator>Saleem, Sadiah</creator><creator>Naseem, Sajida</creator><creator>Ahsan, Fatima</creator><general>Japan Oil Chemists' Society</general><general>Japan Science and Technology Agency</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>F28</scope><scope>FR3</scope><orcidid>https://orcid.org/0000-0002-9211-2944</orcidid><orcidid>https://orcid.org/0000-0001-6506-1080</orcidid><orcidid>https://orcid.org/0000-0001-7098-8649</orcidid><orcidid>https://orcid.org/0000-0002-5218-6471</orcidid><orcidid>https://orcid.org/0000-0002-4638-8253</orcidid><orcidid>https://orcid.org/0000-0002-3754-3135</orcidid><orcidid>https://orcid.org/0000-0002-3909-9242</orcidid></search><sort><creationdate>20220101</creationdate><title>Purification and Characterization of Keratinase from Bacillus licheniformis dcs1 for Poultry Waste Processing</title><author>Liaqat, Iram ; Ali, Sikander ; Butt, Abida ; Durrani, Arjumand Iqbal ; Zafar, Urooj ; Saleem, Sadiah ; Naseem, Sajida ; Ahsan, Fatima</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c630t-29fd427b4bfac796ce78430a9d1d15d0687704127f5638fbf2a9129028de93583</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Animals</topic><topic>B. licheniformis</topic><topic>Bacillus licheniformis - metabolism</topic><topic>Bacteria</topic><topic>Chickens - genetics</topic><topic>Chickens - metabolism</topic><topic>Column chromatography</topic><topic>Degradation</topic><topic>Enzymes</topic><topic>feather degrading bacteria</topic><topic>Feathers</topic><topic>Gene sequencing</topic><topic>Hydrogen-Ion Concentration</topic><topic>Keratin</topic><topic>keratinolytic enzymes</topic><topic>Keratins - analysis</topic><topic>Keratins - metabolism</topic><topic>Peptide Hydrolases - chemistry</topic><topic>Peptide Hydrolases - genetics</topic><topic>Peptide Hydrolases - metabolism</topic><topic>Poultry</topic><topic>Poultry - genetics</topic><topic>Poultry - metabolism</topic><topic>poultry wastes</topic><topic>Purification</topic><topic>RNA, Ribosomal, 16S</topic><topic>Temperature</topic><topic>Waste disposal</topic><toplevel>online_resources</toplevel><creatorcontrib>Liaqat, Iram</creatorcontrib><creatorcontrib>Ali, Sikander</creatorcontrib><creatorcontrib>Butt, Abida</creatorcontrib><creatorcontrib>Durrani, Arjumand Iqbal</creatorcontrib><creatorcontrib>Zafar, Urooj</creatorcontrib><creatorcontrib>Saleem, Sadiah</creatorcontrib><creatorcontrib>Naseem, Sajida</creatorcontrib><creatorcontrib>Ahsan, Fatima</creatorcontrib><creatorcontrib>Microbiology Lab</creatorcontrib><creatorcontrib>University of Veterinary and Animal Sciences</creatorcontrib><creatorcontrib>University of the Punjab</creatorcontrib><creatorcontrib>Department of Chemistry</creatorcontrib><creatorcontrib>Department of Zoology</creatorcontrib><creatorcontrib>Institute of Industrial Biotechnology</creatorcontrib><creatorcontrib>University of Engineering and Technology</creatorcontrib><creatorcontrib>Department of Microbiology</creatorcontrib><creatorcontrib>Division of Science and Technology</creatorcontrib><creatorcontrib>University of Education</creatorcontrib><creatorcontrib>University of Karachi</creatorcontrib><creatorcontrib>Government College University</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><jtitle>Journal of Oleo Science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liaqat, Iram</au><au>Ali, Sikander</au><au>Butt, Abida</au><au>Durrani, Arjumand Iqbal</au><au>Zafar, Urooj</au><au>Saleem, Sadiah</au><au>Naseem, Sajida</au><au>Ahsan, Fatima</au><aucorp>Microbiology Lab</aucorp><aucorp>University of Veterinary and Animal Sciences</aucorp><aucorp>University of the Punjab</aucorp><aucorp>Department of Chemistry</aucorp><aucorp>Department of Zoology</aucorp><aucorp>Institute of Industrial Biotechnology</aucorp><aucorp>University of Engineering and Technology</aucorp><aucorp>Department of Microbiology</aucorp><aucorp>Division of Science and Technology</aucorp><aucorp>University of Education</aucorp><aucorp>University of Karachi</aucorp><aucorp>Government College University</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and Characterization of Keratinase from Bacillus licheniformis dcs1 for Poultry Waste Processing</atitle><jtitle>Journal of Oleo Science</jtitle><addtitle>J Oleo Sci</addtitle><date>2022-01-01</date><risdate>2022</risdate><volume>71</volume><issue>5</issue><spage>693</spage><epage>700</epage><pages>693-700</pages><artnum>ess21426</artnum><issn>1345-8957</issn><eissn>1347-3352</eissn><abstract>Feather wastes-byproduct of commercial poultry processing plant is produced in large amounts. Keratinolytic enzymes produced by feather degrading bacteria can easily degrade these waste products releasing pure keratin as a residue. The aim of present study was to isolate, and characterize feather degrading bacteria as well as assess the keratinolytic potential of purified enzyme. Three feather degrading bacteria (dps3, wps1 and dcs1) were isolated from feathers of domestic chickens. Preliminary characterization of isolated bacteria revealed these isolates belonging to genus Bacillus. 16S rRNA gene sequencing identified the isolates as B. subtilis dps3 (MW255302), B. cereus wps1 (MW255303) and B. licheniformis dcs1 (MW255304). Cell free supernatant of B. licheniformis dcs1 degraded feathers completely in 14 days indicating its keratinolytic ability. Purification of keratinase enzyme from B. licheniformis dcs1 was performed using column chromatography. SDS-PAGE indicated its molecular weight as 32 KDa. Kerotinolytice activity was maximum at optimum pH of 7 and 45℃ temperature. Enzyme showed the potential to degrade keratin material such as hairs and nails of humans. Findings of current study suggested that purified enzyme possess potential to upgrade nutritional quality of poultry waste containing keratin and might play as important biotechnological tool for keratin hydrolysis.</abstract><cop>Japan</cop><pub>Japan Oil Chemists' Society</pub><pmid>35387918</pmid><doi>10.5650/jos.ess21426</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0002-9211-2944</orcidid><orcidid>https://orcid.org/0000-0001-6506-1080</orcidid><orcidid>https://orcid.org/0000-0001-7098-8649</orcidid><orcidid>https://orcid.org/0000-0002-5218-6471</orcidid><orcidid>https://orcid.org/0000-0002-4638-8253</orcidid><orcidid>https://orcid.org/0000-0002-3754-3135</orcidid><orcidid>https://orcid.org/0000-0002-3909-9242</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1345-8957 |
| ispartof | Journal of Oleo Science, 2022, Vol.71(5), pp.693-700 |
| issn | 1345-8957 1347-3352 |
| language | eng |
| recordid | cdi_proquest_journals_2658286037 |
| source | J-STAGE (Free - Japanese); MEDLINE; DOAJ Directory of Open Access Journals; Free Full-Text Journals in Chemistry; EZB* |
| subjects | Animals B. licheniformis Bacillus licheniformis - metabolism Bacteria Chickens - genetics Chickens - metabolism Column chromatography Degradation Enzymes feather degrading bacteria Feathers Gene sequencing Hydrogen-Ion Concentration Keratin keratinolytic enzymes Keratins - analysis Keratins - metabolism Peptide Hydrolases - chemistry Peptide Hydrolases - genetics Peptide Hydrolases - metabolism Poultry Poultry - genetics Poultry - metabolism poultry wastes Purification RNA, Ribosomal, 16S Temperature Waste disposal |
| title | Purification and Characterization of Keratinase from Bacillus licheniformis dcs1 for Poultry Waste Processing |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-28T07%3A15%3A46IST&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=Purification%20and%20Characterization%20of%20Keratinase%20from%20Bacillus%20licheniformis%20dcs1%20for%20Poultry%20Waste%20Processing&rft.jtitle=Journal%20of%20Oleo%20Science&rft.au=Liaqat,%20Iram&rft.aucorp=Microbiology%20Lab&rft.date=2022-01-01&rft.volume=71&rft.issue=5&rft.spage=693&rft.epage=700&rft.pages=693-700&rft.artnum=ess21426&rft.issn=1345-8957&rft.eissn=1347-3352&rft_id=info:doi/10.5650/jos.ess21426&rft_dat=%3Cproquest_cross%3E2658286037%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=2658286037&rft_id=info:pmid/35387918&rfr_iscdi=true |