Optimization of laccase production from Marasimus palmivorus
Laccase is an enzyme that has the ability to oxidize substances. It is one of those enzymes that has innate qualities of reactive radical generation, and its use in many domains has been overlooked due to its commercial unavailability. The ability of Marasimus palmivorus MG717877.1 to produce extrac...
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description | Laccase is an enzyme that has the ability to oxidize substances. It is one of those enzymes that has innate qualities of reactive radical generation, and its use in many domains has been overlooked due to its commercial unavailability. The ability of Marasimus palmivorus MG717877.1 to produce extracellular enzymes (Laccase enzyme) utilizing media containing substrate, named Guaiacol agar medium, was tested. In submerged culture, the ideal pH, incubation duration, and temperature for laccase synthesis were examined. The maximum enzyme activity was reported when the pH of the media was 5.5; laccase activity was (1.03U/ml). The maximum enzyme activity for laccase enzyme was 1.040 U/ml when the temperature was 25°, and (0.922U/ml) after the third day of incubation. |
doi_str_mv | 10.1063/5.0135983 |
format | Conference Proceeding |
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It is one of those enzymes that has innate qualities of reactive radical generation, and its use in many domains has been overlooked due to its commercial unavailability. The ability of Marasimus palmivorus MG717877.1 to produce extracellular enzymes (Laccase enzyme) utilizing media containing substrate, named Guaiacol agar medium, was tested. In submerged culture, the ideal pH, incubation duration, and temperature for laccase synthesis were examined. The maximum enzyme activity was reported when the pH of the media was 5.5; laccase activity was (1.03U/ml). 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The maximum enzyme activity for laccase enzyme was 1.040 U/ml when the temperature was 25°, and (0.922U/ml) after the third day of incubation.</description><subject>Enzyme activity</subject><subject>Enzymes</subject><subject>Laccase</subject><subject>Optimization</subject><subject>Substrates</subject><issn>0094-243X</issn><issn>1551-7616</issn><fulltext>true</fulltext><rsrctype>conference_proceeding</rsrctype><creationdate>2023</creationdate><recordtype>conference_proceeding</recordtype><recordid>eNp9kE1LxDAQhoMouK4e_AcFb0LXyaRJGvAii1-wshcFbyFtGsjSbmPSCvrrrbsL3oSBgZlnZt55CbmksKAg2A1fAGVcleyIzCjnNJeCimMyA1BFjgV7PyVnKW0AUElZzsjtOgy-899m8P02613Wmro2qclC7O1Y76ou9l32YqJJvhtTFkzb-c8-jumcnDjTpubikOfk7eH-dfmUr9aPz8u7VR4QGMuFrR0XCNUUDlUNTVkYQOaYVajQTQ0E6lAIC-CKqiq4QuRoDTNUCGRzcrXfO4n6GJs06E0_xu10UqNUqpTIJUzU9Z5KtR92_-gQfWfil57Uaq4Pzuhg3X8wBf1r5d8A-wH0imSM</recordid><startdate>20230412</startdate><enddate>20230412</enddate><creator>Mohsen, Liqaa Y.</creator><creator>Lilo, Rafal Ahmed</creator><creator>AL-Maamori, Anmar Mahdi Kadhum</creator><general>American Institute of Physics</general><scope>8FD</scope><scope>H8D</scope><scope>L7M</scope></search><sort><creationdate>20230412</creationdate><title>Optimization of laccase production from Marasimus palmivorus</title><author>Mohsen, Liqaa Y. ; Lilo, Rafal Ahmed ; AL-Maamori, Anmar Mahdi Kadhum</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p2033-6dcf5620b20bf29c0e84a023f3d9292f0b2201f266d00f4bb4592252da3a16623</frbrgroupid><rsrctype>conference_proceedings</rsrctype><prefilter>conference_proceedings</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Enzyme activity</topic><topic>Enzymes</topic><topic>Laccase</topic><topic>Optimization</topic><topic>Substrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mohsen, Liqaa Y.</creatorcontrib><creatorcontrib>Lilo, Rafal Ahmed</creatorcontrib><creatorcontrib>AL-Maamori, Anmar Mahdi Kadhum</creatorcontrib><collection>Technology Research Database</collection><collection>Aerospace Database</collection><collection>Advanced Technologies Database with Aerospace</collection></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mohsen, Liqaa Y.</au><au>Lilo, Rafal Ahmed</au><au>AL-Maamori, Anmar Mahdi Kadhum</au><au>Al-Shamani, Ali Najah</au><au>Abid, Dhurgham Hassan</au><au>Wadday, Ahmed Ghanim</au><au>Ibadi, Atheer Kadhim</au><au>Alsaffar, Marwa Fadhil</au><au>Jaaz, Hussein Abad Gazi</au><au>Ali, Faris Mohammed</au><au>AL-Hasnawi, Dhafer Manea Hachim</au><au>Al-Manea, Ahmed Razzaq Hasan</au><au>Alsultani, Saadia H Kadhim</au><format>book</format><genre>proceeding</genre><ristype>CONF</ristype><atitle>Optimization of laccase production from Marasimus palmivorus</atitle><btitle>AIP Conference Proceedings</btitle><date>2023-04-12</date><risdate>2023</risdate><volume>2776</volume><issue>1</issue><issn>0094-243X</issn><eissn>1551-7616</eissn><coden>APCPCS</coden><abstract>Laccase is an enzyme that has the ability to oxidize substances. It is one of those enzymes that has innate qualities of reactive radical generation, and its use in many domains has been overlooked due to its commercial unavailability. The ability of Marasimus palmivorus MG717877.1 to produce extracellular enzymes (Laccase enzyme) utilizing media containing substrate, named Guaiacol agar medium, was tested. In submerged culture, the ideal pH, incubation duration, and temperature for laccase synthesis were examined. The maximum enzyme activity was reported when the pH of the media was 5.5; laccase activity was (1.03U/ml). The maximum enzyme activity for laccase enzyme was 1.040 U/ml when the temperature was 25°, and (0.922U/ml) after the third day of incubation.</abstract><cop>Melville</cop><pub>American Institute of Physics</pub><doi>10.1063/5.0135983</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Enzyme activity Enzymes Laccase Optimization Substrates |
title | Optimization of laccase production from Marasimus palmivorus |
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