Expression of lignin peroxidase H2 from Phanerochaete chrysosporium by multi-copy recombinant Pichia strain.
Identifieur interne : 000630 ( Main/Exploration ); précédent : 000629; suivant : 000631Expression of lignin peroxidase H2 from Phanerochaete chrysosporium by multi-copy recombinant Pichia strain.
Auteurs : Wei Wang [République populaire de Chine] ; Xianghua WenSource :
- Journal of environmental sciences (China) [ 1001-0742 ] ; 2009.
Descripteurs français
- KwdFr :
- Analyse de séquence d'ADN (MeSH), Clonage moléculaire (MeSH), Dosage génique (MeSH), Isoenzymes (génétique), Peroxidases (métabolisme), Phanerochaete (enzymologie), Pichia (génétique), Pichia (métabolisme), Plasmides (génétique), Vecteurs génétiques (MeSH), Électrophorèse sur gel d'agar (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- enzymologie : Phanerochaete.
- génétique : Isoenzymes, Pichia, Plasmides.
- métabolisme : Peroxidases, Pichia.
- Analyse de séquence d'ADN, Clonage moléculaire, Dosage génique, Vecteurs génétiques, Électrophorèse sur gel d'agar, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Cloning, Molecular (MeSH), Electrophoresis, Agar Gel (MeSH), Electrophoresis, Polyacrylamide Gel (MeSH), Gene Dosage (MeSH), Genetic Vectors (MeSH), Isoenzymes (genetics), Peroxidases (metabolism), Phanerochaete (enzymology), Pichia (genetics), Pichia (metabolism), Plasmids (genetics), Sequence Analysis, DNA (MeSH).
- MESH :
- chemical , genetics : Isoenzymes.
- chemical , metabolism : Peroxidases.
- enzymology : Phanerochaete.
- genetics : Pichia, Plasmids.
- metabolism : Pichia.
- Cloning, Molecular, Electrophoresis, Agar Gel, Electrophoresis, Polyacrylamide Gel, Gene Dosage, Genetic Vectors, Sequence Analysis, DNA.
Abstract
The lipH2 gene, encoding the expression of lignin peroxidase, was cloned from Phanerochaete chrysosporium BKM-F-1767 and expressed in Pichia pastoris X-33, a yeast. The cDNA of LiPH2 was generated from total RNA extracted from P. chrysosporium by PCR with primers that do not contain a P. chrysosporium lignin peroxidase secretion signal. The gene was then successfully inserted into the expression vector pPICZalpha, and resulted in the recombinant vector pPICZalpha-lipH2. The transformation was conducted in two ways. One was using the wild Pichia pastoris as the recipients, which results in the recombinant P. pastoris with single or low lipH2 gene copy. The second was using P. pastoris and single or low lipH2 gene copy as the recipients, which results in the recombinant P. pastoris with multi-copies of lipH2 genes. This study firstly expressed the gene lipH2 in P. pastoris and achieved the successful expression of the lipH2 depending upon the generation of a recombinant strain that contained multiple copies. The lignin peroxidase activity reached a maximum of 15 U/L after 12 h induction.
DOI: 10.1016/s1001-0742(08)62254-8
PubMed: 19402425
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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d'agar</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The lipH2 gene, encoding the expression of lignin peroxidase, was cloned from Phanerochaete chrysosporium BKM-F-1767 and expressed in Pichia pastoris X-33, a yeast. The cDNA of LiPH2 was generated from total RNA extracted from P. chrysosporium by PCR with primers that do not contain a P. chrysosporium lignin peroxidase secretion signal. The gene was then successfully inserted into the expression vector pPICZalpha, and resulted in the recombinant vector pPICZalpha-lipH2. The transformation was conducted in two ways. One was using the wild Pichia pastoris as the recipients, which results in the recombinant P. pastoris with single or low lipH2 gene copy. The second was using P. pastoris and single or low lipH2 gene copy as the recipients, which results in the recombinant P. pastoris with multi-copies of lipH2 genes. This study firstly expressed the gene lipH2 in P. pastoris and achieved the successful expression of the lipH2 depending upon the generation of a recombinant strain that contained multiple copies. The lignin peroxidase activity reached a maximum of 15 U/L after 12 h induction.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19402425</PMID><DateCompleted><Year>2009</Year><Month>05</Month><Day>19</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>11</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1001-0742</ISSN><JournalIssue CitedMedium="Print"><Volume>21</Volume><Issue>2</Issue><PubDate><Year>2009</Year></PubDate></JournalIssue><Title>Journal of environmental sciences (China)</Title><ISOAbbreviation>J Environ Sci (China)</ISOAbbreviation></Journal><ArticleTitle>Expression of lignin peroxidase H2 from Phanerochaete chrysosporium by multi-copy recombinant Pichia strain.</ArticleTitle><Pagination><MedlinePgn>218-22</MedlinePgn></Pagination><Abstract><AbstractText>The lipH2 gene, encoding the expression of lignin peroxidase, was cloned from Phanerochaete chrysosporium BKM-F-1767 and expressed in Pichia pastoris X-33, a yeast. The cDNA of LiPH2 was generated from total RNA extracted from P. chrysosporium by PCR with primers that do not contain a P. chrysosporium lignin peroxidase secretion signal. The gene was then successfully inserted into the expression vector pPICZalpha, and resulted in the recombinant vector pPICZalpha-lipH2. The transformation was conducted in two ways. One was using the wild Pichia pastoris as the recipients, which results in the recombinant P. pastoris with single or low lipH2 gene copy. The second was using P. pastoris and single or low lipH2 gene copy as the recipients, which results in the recombinant P. pastoris with multi-copies of lipH2 genes. This study firstly expressed the gene lipH2 in P. pastoris and achieved the successful expression of the lipH2 depending upon the generation of a recombinant strain that contained multiple copies. 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