Production, purification, and characterization of p-diphenol oxidase (PDO) enzyme from lignolytic fungal isolate Schizophyllum commune MF-O5
Fungi are producers of lignolytic extracellular enzymes which are used in industries like textile, detergents, biorefineries, and paper pulping. This study assessed for the production, purification, and characterization of novel p -diphenol oxidase (PDO; laccase) enzyme from lignolytic white-rot fun...
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| Veröffentlicht in: | Folia microbiologica 2023-12, Vol.68 (6), p.867-888 |
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| creator | Faheem, Muhammad Bokhari, Syed Ali Imran Malik, Muhammad Arshad Ahmad, Bashir Riaz, Muhammad Zahid, Nafeesa Hussain, Adil Ghani, Abdul Ullah, Hanif Shah, Waseem Mehmood, Rashid Ahmad, Khurshid Rasheed, Hassam Zain, Ali Hussain, Saddam Khan, Abrar Yasin, Muhammad Talha Tariq, Hasnat Rizwanullah Basheir, Muhammad Mudassir Jogezai, NaqeebUllah |
| description | Fungi are producers of lignolytic extracellular enzymes which are used in industries like textile, detergents, biorefineries, and paper pulping. This study assessed for the production, purification, and characterization of novel
p
-diphenol oxidase (PDO; laccase) enzyme from lignolytic white-rot fungal isolate. Fungi samples collected from different areas of Pakistan were initially screened using guaiacol plate method. The maximum PDO producing fungal isolate was identified on the basis of ITS (internal transcribed spacer sequence of DNA of ribosomal RNA) sequencing. To get optimum enzyme yield, various growth and fermentation conditions were optimized. Later PDO was purified using ammonium sulfate precipitation, size exclusion, and anion exchange chromatography and characterized. It was observed that the maximum PDO producing fungal isolate was
Schizophyllum commune
(MF-O5). Characterization results showed that the purified PDO was a monomeric protein with a molecular mass of 68 kDa and showed stability at lower temperature (30 °C) for 1 h. The
K
m
and
V
max
values of the purified PDO recorded were 2.48 mM and 6.20 U/min. Thermal stability results showed that at 30 °C PDO had 119.17 kJ/K/mol
E
a
value and 33.64 min half-life. The PDO activity was stimulated by Cu
2+
ion at 1.0 mM showing enhanced activity up to 111.04%. Strong inhibition effect was noted for Fe
2+
ions at 1 mM showing 12.04% activity. The enzyme showed stability against 10 mM concentration oxidizing reducing agents like DMSO, EDTA, H
2
O
2
, NaOCl, and urea and retained more than 75% of relative activity. The characterization of purified PDO enzyme confirmed its tolerance against salt, metal ions, organic solvents, and surfactants indicating its ability to be used in the versatile commercial applications. |
| doi_str_mv | 10.1007/s12223-023-01056-w |
| format | Article |
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p
-diphenol oxidase (PDO; laccase) enzyme from lignolytic white-rot fungal isolate. Fungi samples collected from different areas of Pakistan were initially screened using guaiacol plate method. The maximum PDO producing fungal isolate was identified on the basis of ITS (internal transcribed spacer sequence of DNA of ribosomal RNA) sequencing. To get optimum enzyme yield, various growth and fermentation conditions were optimized. Later PDO was purified using ammonium sulfate precipitation, size exclusion, and anion exchange chromatography and characterized. It was observed that the maximum PDO producing fungal isolate was
Schizophyllum commune
(MF-O5). Characterization results showed that the purified PDO was a monomeric protein with a molecular mass of 68 kDa and showed stability at lower temperature (30 °C) for 1 h. The
K
m
and
V
max
values of the purified PDO recorded were 2.48 mM and 6.20 U/min. Thermal stability results showed that at 30 °C PDO had 119.17 kJ/K/mol
E
a
value and 33.64 min half-life. The PDO activity was stimulated by Cu
2+
ion at 1.0 mM showing enhanced activity up to 111.04%. Strong inhibition effect was noted for Fe
2+
ions at 1 mM showing 12.04% activity. The enzyme showed stability against 10 mM concentration oxidizing reducing agents like DMSO, EDTA, H
2
O
2
, NaOCl, and urea and retained more than 75% of relative activity. The characterization of purified PDO enzyme confirmed its tolerance against salt, metal ions, organic solvents, and surfactants indicating its ability to be used in the versatile commercial applications.</description><identifier>ISSN: 0015-5632</identifier><identifier>ISSN: 1874-9356</identifier><identifier>EISSN: 1874-9356</identifier><identifier>DOI: 10.1007/s12223-023-01056-w</identifier><identifier>PMID: 37160524</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Ammonium ; Ammonium sulfate ; Anion exchange ; anion exchange chromatography ; Anion exchanging ; Applied Microbiology ; Biomedical and Life Sciences ; Biorefineries ; biorefining ; Copper ; Detergents ; Diphenols ; DNA ; DNA sequencing ; Environmental Engineering/Biotechnology ; Enzyme Stability ; Enzymes ; Ethylenediaminetetraacetic acids ; Extracellular enzymes ; fabrics ; Fermentation ; Fungi ; Guaiacol ; half life ; Hydrogen Peroxide ; Hydrogen-Ion Concentration ; Immunology ; internal transcribed spacers ; laccase ; Laccase - metabolism ; Life Sciences ; Low temperature ; Metal ions ; Microbiology ; molecular weight ; Nucleotide sequence ; Organic solvents ; Original Article ; Oxidase ; Pakistan ; Pulping ; Purification ; Reducing agents ; ribosomal RNA ; rRNA ; Schizophyllum - genetics ; Schizophyllum - metabolism ; Schizophyllum commune ; Sodium hypochlorite ; Temperature ; Thermal stability ; Urea ; White rot</subject><ispartof>Folia microbiologica, 2023-12, Vol.68 (6), p.867-888</ispartof><rights>Institute of Microbiology, Academy of Sciences of the Czech Republic, v.v.i. 2023. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2023. Institute of Microbiology, Academy of Sciences of the Czech Republic, v.v.i.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c359t-53b53525fe4bfe1e19b533ae460179b6485e925ed06973688fac98ca7e1acc9c3</cites><orcidid>0000-0003-3347-765X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12223-023-01056-w$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12223-023-01056-w$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37160524$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Faheem, Muhammad</creatorcontrib><creatorcontrib>Bokhari, Syed Ali Imran</creatorcontrib><creatorcontrib>Malik, Muhammad Arshad</creatorcontrib><creatorcontrib>Ahmad, Bashir</creatorcontrib><creatorcontrib>Riaz, Muhammad</creatorcontrib><creatorcontrib>Zahid, Nafeesa</creatorcontrib><creatorcontrib>Hussain, Adil</creatorcontrib><creatorcontrib>Ghani, Abdul</creatorcontrib><creatorcontrib>Ullah, Hanif</creatorcontrib><creatorcontrib>Shah, Waseem</creatorcontrib><creatorcontrib>Mehmood, Rashid</creatorcontrib><creatorcontrib>Ahmad, Khurshid</creatorcontrib><creatorcontrib>Rasheed, Hassam</creatorcontrib><creatorcontrib>Zain, Ali</creatorcontrib><creatorcontrib>Hussain, Saddam</creatorcontrib><creatorcontrib>Khan, Abrar</creatorcontrib><creatorcontrib>Yasin, Muhammad Talha</creatorcontrib><creatorcontrib>Tariq, Hasnat</creatorcontrib><creatorcontrib>Rizwanullah</creatorcontrib><creatorcontrib>Basheir, Muhammad Mudassir</creatorcontrib><creatorcontrib>Jogezai, NaqeebUllah</creatorcontrib><title>Production, purification, and characterization of p-diphenol oxidase (PDO) enzyme from lignolytic fungal isolate Schizophyllum commune MF-O5</title><title>Folia microbiologica</title><addtitle>Folia Microbiol</addtitle><addtitle>Folia Microbiol (Praha)</addtitle><description>Fungi are producers of lignolytic extracellular enzymes which are used in industries like textile, detergents, biorefineries, and paper pulping. This study assessed for the production, purification, and characterization of novel
p
-diphenol oxidase (PDO; laccase) enzyme from lignolytic white-rot fungal isolate. Fungi samples collected from different areas of Pakistan were initially screened using guaiacol plate method. The maximum PDO producing fungal isolate was identified on the basis of ITS (internal transcribed spacer sequence of DNA of ribosomal RNA) sequencing. To get optimum enzyme yield, various growth and fermentation conditions were optimized. Later PDO was purified using ammonium sulfate precipitation, size exclusion, and anion exchange chromatography and characterized. It was observed that the maximum PDO producing fungal isolate was
Schizophyllum commune
(MF-O5). Characterization results showed that the purified PDO was a monomeric protein with a molecular mass of 68 kDa and showed stability at lower temperature (30 °C) for 1 h. The
K
m
and
V
max
values of the purified PDO recorded were 2.48 mM and 6.20 U/min. Thermal stability results showed that at 30 °C PDO had 119.17 kJ/K/mol
E
a
value and 33.64 min half-life. The PDO activity was stimulated by Cu
2+
ion at 1.0 mM showing enhanced activity up to 111.04%. Strong inhibition effect was noted for Fe
2+
ions at 1 mM showing 12.04% activity. The enzyme showed stability against 10 mM concentration oxidizing reducing agents like DMSO, EDTA, H
2
O
2
, NaOCl, and urea and retained more than 75% of relative activity. The characterization of purified PDO enzyme confirmed its tolerance against salt, metal ions, organic solvents, and surfactants indicating its ability to be used in the versatile commercial applications.</description><subject>Ammonium</subject><subject>Ammonium sulfate</subject><subject>Anion exchange</subject><subject>anion exchange chromatography</subject><subject>Anion exchanging</subject><subject>Applied Microbiology</subject><subject>Biomedical and Life Sciences</subject><subject>Biorefineries</subject><subject>biorefining</subject><subject>Copper</subject><subject>Detergents</subject><subject>Diphenols</subject><subject>DNA</subject><subject>DNA sequencing</subject><subject>Environmental Engineering/Biotechnology</subject><subject>Enzyme Stability</subject><subject>Enzymes</subject><subject>Ethylenediaminetetraacetic acids</subject><subject>Extracellular enzymes</subject><subject>fabrics</subject><subject>Fermentation</subject><subject>Fungi</subject><subject>Guaiacol</subject><subject>half life</subject><subject>Hydrogen Peroxide</subject><subject>Hydrogen-Ion Concentration</subject><subject>Immunology</subject><subject>internal transcribed spacers</subject><subject>laccase</subject><subject>Laccase - metabolism</subject><subject>Life Sciences</subject><subject>Low temperature</subject><subject>Metal ions</subject><subject>Microbiology</subject><subject>molecular weight</subject><subject>Nucleotide sequence</subject><subject>Organic solvents</subject><subject>Original Article</subject><subject>Oxidase</subject><subject>Pakistan</subject><subject>Pulping</subject><subject>Purification</subject><subject>Reducing agents</subject><subject>ribosomal RNA</subject><subject>rRNA</subject><subject>Schizophyllum - genetics</subject><subject>Schizophyllum - metabolism</subject><subject>Schizophyllum commune</subject><subject>Sodium hypochlorite</subject><subject>Temperature</subject><subject>Thermal stability</subject><subject>Urea</subject><subject>White rot</subject><issn>0015-5632</issn><issn>1874-9356</issn><issn>1874-9356</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkc-KFDEQh4Mo7rj6Ah4k4GUFo_nTSXeOsroqrMyCem4y6eqZLOmkTbpZZ57BhzazvSp40EMRKvnqK8IPoaeMvmKU1q8z45wLQo_FqFTk5h5asaauiBZS3UcrSpkkUgl-gh7lfE2popXgD9GJqJmiklcr9OMqxW62k4vhJR7n5HpnzdKZ0GG7M8nYCZI73N7i2OORdG7cQYgex--uMxnw2dXb9QsM4bAfAPcpDti7bQH2k7O4n8PWeOxy9GYC_Nnu3CGOu73384BtHIY5AP50QdbyMXrQG5_hyd15ir5evPty_oFcrt9_PH9zSayQeiJSbKSQXPZQbXpgwHTphYFKUVbrjaoaCZpL6KjStVBN0xurG2tqYMZabcUpOlu8Y4rfZshTO7hswXsTIM65Faz460op8V-UN4zpimrNCvr8L_Q6zimUjxRKS1k31a2QL5RNMecEfTsmN5i0bxltj7G2S6wtPdYx1vamDD27U8-bAbrfI79yLIBYgFyewhbSn93_0P4EgPeuwg</recordid><startdate>20231201</startdate><enddate>20231201</enddate><creator>Faheem, 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purification, and characterization of p-diphenol oxidase (PDO) enzyme from lignolytic fungal isolate Schizophyllum commune MF-O5</title><author>Faheem, Muhammad ; Bokhari, Syed Ali Imran ; Malik, Muhammad Arshad ; Ahmad, Bashir ; Riaz, Muhammad ; Zahid, Nafeesa ; Hussain, Adil ; Ghani, Abdul ; Ullah, Hanif ; Shah, Waseem ; Mehmood, Rashid ; Ahmad, Khurshid ; Rasheed, Hassam ; Zain, Ali ; Hussain, Saddam ; Khan, Abrar ; Yasin, Muhammad Talha ; Tariq, Hasnat ; Rizwanullah ; Basheir, Muhammad Mudassir ; Jogezai, NaqeebUllah</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c359t-53b53525fe4bfe1e19b533ae460179b6485e925ed06973688fac98ca7e1acc9c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Ammonium</topic><topic>Ammonium sulfate</topic><topic>Anion exchange</topic><topic>anion exchange chromatography</topic><topic>Anion exchanging</topic><topic>Applied Microbiology</topic><topic>Biomedical and Life Sciences</topic><topic>Biorefineries</topic><topic>biorefining</topic><topic>Copper</topic><topic>Detergents</topic><topic>Diphenols</topic><topic>DNA</topic><topic>DNA sequencing</topic><topic>Environmental Engineering/Biotechnology</topic><topic>Enzyme Stability</topic><topic>Enzymes</topic><topic>Ethylenediaminetetraacetic acids</topic><topic>Extracellular enzymes</topic><topic>fabrics</topic><topic>Fermentation</topic><topic>Fungi</topic><topic>Guaiacol</topic><topic>half life</topic><topic>Hydrogen Peroxide</topic><topic>Hydrogen-Ion Concentration</topic><topic>Immunology</topic><topic>internal transcribed spacers</topic><topic>laccase</topic><topic>Laccase - metabolism</topic><topic>Life Sciences</topic><topic>Low temperature</topic><topic>Metal ions</topic><topic>Microbiology</topic><topic>molecular weight</topic><topic>Nucleotide sequence</topic><topic>Organic solvents</topic><topic>Original Article</topic><topic>Oxidase</topic><topic>Pakistan</topic><topic>Pulping</topic><topic>Purification</topic><topic>Reducing agents</topic><topic>ribosomal RNA</topic><topic>rRNA</topic><topic>Schizophyllum - genetics</topic><topic>Schizophyllum - metabolism</topic><topic>Schizophyllum commune</topic><topic>Sodium hypochlorite</topic><topic>Temperature</topic><topic>Thermal stability</topic><topic>Urea</topic><topic>White rot</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Faheem, Muhammad</creatorcontrib><creatorcontrib>Bokhari, Syed Ali Imran</creatorcontrib><creatorcontrib>Malik, Muhammad Arshad</creatorcontrib><creatorcontrib>Ahmad, Bashir</creatorcontrib><creatorcontrib>Riaz, Muhammad</creatorcontrib><creatorcontrib>Zahid, Nafeesa</creatorcontrib><creatorcontrib>Hussain, Adil</creatorcontrib><creatorcontrib>Ghani, Abdul</creatorcontrib><creatorcontrib>Ullah, Hanif</creatorcontrib><creatorcontrib>Shah, 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Ali</au><au>Hussain, Saddam</au><au>Khan, Abrar</au><au>Yasin, Muhammad Talha</au><au>Tariq, Hasnat</au><au>Rizwanullah</au><au>Basheir, Muhammad Mudassir</au><au>Jogezai, NaqeebUllah</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Production, purification, and characterization of p-diphenol oxidase (PDO) enzyme from lignolytic fungal isolate Schizophyllum commune MF-O5</atitle><jtitle>Folia microbiologica</jtitle><stitle>Folia Microbiol</stitle><addtitle>Folia Microbiol (Praha)</addtitle><date>2023-12-01</date><risdate>2023</risdate><volume>68</volume><issue>6</issue><spage>867</spage><epage>888</epage><pages>867-888</pages><issn>0015-5632</issn><issn>1874-9356</issn><eissn>1874-9356</eissn><abstract>Fungi are producers of lignolytic extracellular enzymes which are used in industries like textile, detergents, biorefineries, and paper pulping. This study assessed for the production, purification, and characterization of novel
p
-diphenol oxidase (PDO; laccase) enzyme from lignolytic white-rot fungal isolate. Fungi samples collected from different areas of Pakistan were initially screened using guaiacol plate method. The maximum PDO producing fungal isolate was identified on the basis of ITS (internal transcribed spacer sequence of DNA of ribosomal RNA) sequencing. To get optimum enzyme yield, various growth and fermentation conditions were optimized. Later PDO was purified using ammonium sulfate precipitation, size exclusion, and anion exchange chromatography and characterized. It was observed that the maximum PDO producing fungal isolate was
Schizophyllum commune
(MF-O5). Characterization results showed that the purified PDO was a monomeric protein with a molecular mass of 68 kDa and showed stability at lower temperature (30 °C) for 1 h. The
K
m
and
V
max
values of the purified PDO recorded were 2.48 mM and 6.20 U/min. Thermal stability results showed that at 30 °C PDO had 119.17 kJ/K/mol
E
a
value and 33.64 min half-life. The PDO activity was stimulated by Cu
2+
ion at 1.0 mM showing enhanced activity up to 111.04%. Strong inhibition effect was noted for Fe
2+
ions at 1 mM showing 12.04% activity. The enzyme showed stability against 10 mM concentration oxidizing reducing agents like DMSO, EDTA, H
2
O
2
, NaOCl, and urea and retained more than 75% of relative activity. The characterization of purified PDO enzyme confirmed its tolerance against salt, metal ions, organic solvents, and surfactants indicating its ability to be used in the versatile commercial applications.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>37160524</pmid><doi>10.1007/s12223-023-01056-w</doi><tpages>22</tpages><orcidid>https://orcid.org/0000-0003-3347-765X</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0015-5632 |
| ispartof | Folia microbiologica, 2023-12, Vol.68 (6), p.867-888 |
| issn | 0015-5632 1874-9356 1874-9356 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_3153574663 |
| source | MEDLINE; Springer Nature - Complete Springer Journals |
| subjects | Ammonium Ammonium sulfate Anion exchange anion exchange chromatography Anion exchanging Applied Microbiology Biomedical and Life Sciences Biorefineries biorefining Copper Detergents Diphenols DNA DNA sequencing Environmental Engineering/Biotechnology Enzyme Stability Enzymes Ethylenediaminetetraacetic acids Extracellular enzymes fabrics Fermentation Fungi Guaiacol half life Hydrogen Peroxide Hydrogen-Ion Concentration Immunology internal transcribed spacers laccase Laccase - metabolism Life Sciences Low temperature Metal ions Microbiology molecular weight Nucleotide sequence Organic solvents Original Article Oxidase Pakistan Pulping Purification Reducing agents ribosomal RNA rRNA Schizophyllum - genetics Schizophyllum - metabolism Schizophyllum commune Sodium hypochlorite Temperature Thermal stability Urea White rot |
| title | Production, purification, and characterization of p-diphenol oxidase (PDO) enzyme from lignolytic fungal isolate Schizophyllum commune MF-O5 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-30T16%3A17%3A42IST&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=Production,%20purification,%20and%20characterization%20of%20p-diphenol%20oxidase%20(PDO)%20enzyme%20from%20lignolytic%20fungal%20isolate%20Schizophyllum%20commune%20MF-O5&rft.jtitle=Folia%20microbiologica&rft.au=Faheem,%20Muhammad&rft.date=2023-12-01&rft.volume=68&rft.issue=6&rft.spage=867&rft.epage=888&rft.pages=867-888&rft.issn=0015-5632&rft.eissn=1874-9356&rft_id=info:doi/10.1007/s12223-023-01056-w&rft_dat=%3Cproquest_cross%3E3153574663%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=2895578463&rft_id=info:pmid/37160524&rfr_iscdi=true |