Improved catalytic activities of a dye-decolorizing peroxidase (DyP) by overexpression of ALA and heme biosynthesis genes in Escherichia coli
DC Field | Value | Language |
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dc.contributor.author | Ramzi, Ahmad Bazli | - |
dc.contributor.author | Hyeon, Jeong Eun | - |
dc.contributor.author | Han, Sung Ok | - |
dc.date.accessioned | 2021-09-04T13:58:42Z | - |
dc.date.available | 2021-09-04T13:58:42Z | - |
dc.date.created | 2021-06-18 | - |
dc.date.issued | 2015-08 | - |
dc.identifier.issn | 1359-5113 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/92925 | - |
dc.description.abstract | Hemoproteins are biotechnologically important heme-containing enzymes, and their production often requires optimal supply of precursors, such as 5-aminolevulinic acid (ALA) and hemin. In this work, endogenous ALA biosynthesis in Escherichia coil was increased as a strategy to improve catalytic activities of a recombinant dye-decolorizing peroxidase (DyP) from Bacillus subtilis. The positive effects of this expression system (pHemAL-DyP) are compared with individually expressed DyP strains grown with (pDyP + Hemin) and without (pDyP) the addition of hemin. The pHemAL-DyP plasmid increased intracellular ALA up to 117.5 mg/L, a 4.0-fold increased from control strain (pET22b, 29.7 mg/L of ALA). Soret peak in the UV-vis spectra was the highest for pHemAL-DyP strain with Reinheitszahl (A(408)/A(280)) value of 0.65 indicating higher heme content in the DyP produced compared to pDyP (0.39) and pDyP + Hemin (0.46). Peroxidase activity was increased-up to 66.7 U/mg in the pHemAL-DyP strain compared to 39.0 and 43.4 U/mg for pDyP and pDyP + Hemin, respectively. Decolorization percentage of Reactive Blue 19 dye was the highest in the pHemAL-DyP strain with 84.7% as compared to the pDyP (69.9%) and pDyP + Hemin (72.8%) systems. In brief, enzymatic properties of recombinant DyP were successfully enhanced using this genetic engineering strategy thus eliminating the need for costly exogenous precursors. (C) 2015 Elsevier Ltd. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ELSEVIER SCI LTD | - |
dc.subject | TRANSFER-RNA REDUCTASE | - |
dc.subject | SACCHAROMYCES-CEREVISIAE | - |
dc.subject | 5-AMINOLEVULINIC ACID | - |
dc.subject | HUMAN HEMOGLOBIN | - |
dc.subject | HETEROLOGOUS EXPRESSION | - |
dc.subject | HORSERADISH-PEROXIDASE | - |
dc.subject | SALMONELLA-TYPHIMURIUM | - |
dc.subject | FUNCTIONAL EXPRESSION | - |
dc.subject | MANGANESE PEROXIDASE | - |
dc.subject | PICHIA-PASTORIS | - |
dc.title | Improved catalytic activities of a dye-decolorizing peroxidase (DyP) by overexpression of ALA and heme biosynthesis genes in Escherichia coli | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Han, Sung Ok | - |
dc.identifier.doi | 10.1016/j.procbio.2015.05.004 | - |
dc.identifier.scopusid | 2-s2.0-84933279626 | - |
dc.identifier.wosid | 000358700100013 | - |
dc.identifier.bibliographicCitation | PROCESS BIOCHEMISTRY, v.50, no.8, pp.1272 - 1276 | - |
dc.relation.isPartOf | PROCESS BIOCHEMISTRY | - |
dc.citation.title | PROCESS BIOCHEMISTRY | - |
dc.citation.volume | 50 | - |
dc.citation.number | 8 | - |
dc.citation.startPage | 1272 | - |
dc.citation.endPage | 1276 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biotechnology & Applied Microbiology | - |
dc.relation.journalResearchArea | Engineering | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biotechnology & Applied Microbiology | - |
dc.relation.journalWebOfScienceCategory | Engineering, Chemical | - |
dc.subject.keywordPlus | TRANSFER-RNA REDUCTASE | - |
dc.subject.keywordPlus | SACCHAROMYCES-CEREVISIAE | - |
dc.subject.keywordPlus | 5-AMINOLEVULINIC ACID | - |
dc.subject.keywordPlus | HUMAN HEMOGLOBIN | - |
dc.subject.keywordPlus | HETEROLOGOUS EXPRESSION | - |
dc.subject.keywordPlus | HORSERADISH-PEROXIDASE | - |
dc.subject.keywordPlus | SALMONELLA-TYPHIMURIUM | - |
dc.subject.keywordPlus | FUNCTIONAL EXPRESSION | - |
dc.subject.keywordPlus | MANGANESE PEROXIDASE | - |
dc.subject.keywordPlus | PICHIA-PASTORIS | - |
dc.subject.keywordAuthor | Dye-decolorizing peroxidase | - |
dc.subject.keywordAuthor | Dye-decolorization | - |
dc.subject.keywordAuthor | 5-Aminolevulinic acid | - |
dc.subject.keywordAuthor | Heme peroxidase | - |
dc.subject.keywordAuthor | Hemoprotein | - |
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