Identification, characterization, and purification of xylanase PC-01 isolated from Pacet hot spring

dc.creatorNi Nyoman Purwani, Mamik Damayanti,
dc.creatorDwi Purwadi, Ni Made
dc.creatorFithri, Lailatul
dc.date2019-12-31
dc.date.accessioned2022-11-05T02:27:55Z
dc.date.available2022-11-05T02:27:55Z
dc.identifierhttps://produccioncientificaluz.org/index.php/opcion/article/view/30731
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/5141379
dc.descriptionThis research aims to characterize, identify and purify the xylanolytic enzymes by hydrophobic interaction and anion exchange chromatography via the endo-β-xylanase activity test with the DNS method. The best results obtained from anion-exchange chromatography of third fraction pH 5 with the purity level of 78.25 times higher than crude extract. In conclusion, Characteristics of bacterial isolates PC-01 are rod-shaped bacterial cells, Gram-positive, and have subterminal oval endospores.es-ES
dc.formatapplication/pdf
dc.languagespa
dc.publisherUniversidad del Zuliaes-ES
dc.relationhttps://produccioncientificaluz.org/index.php/opcion/article/view/30731/31780
dc.rightsDerechos de autor 2019 Opciónes-ES
dc.sourceOpción; Vol. 35 (2019): Edición Especial Nro. 24; 1074-1091es-ES
dc.source2477-9385
dc.source1012-1587
dc.subjectEndo-Β-Xylanasees-ES
dc.subjectHydrophobices-ES
dc.subjectInteractionses-ES
dc.subjectChromatographyes-ES
dc.titleIdentification, characterization, and purification of xylanase PC-01 isolated from Pacet hot springes-ES
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:eu-repo/semantics/publishedVersion
dc.typeArtículo revisado por pareses-ES


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