The brown-rot basidiomycete Fomitopsis palustris has the endo-glucanases capable of degrading microcrystalline cellulose.
Identifieur interne : 000716 ( Main/Exploration ); précédent : 000715; suivant : 000717The brown-rot basidiomycete Fomitopsis palustris has the endo-glucanases capable of degrading microcrystalline cellulose.
Auteurs : Jeong-Jun Yoon [Corée du Sud] ; Chang-Jun Cha ; Yeong-Suk Kim ; Dong-Won Son ; Young-Kyoon KimSource :
- Journal of microbiology and biotechnology [ 1017-7825 ] ; 2007.
Descripteurs français
- KwdFr :
- Analyse de séquence de protéine (MeSH), Basidiomycota (enzymologie), Carboxyméthylcellulose de sodium (métabolisme), Cellobiose (métabolisme), Cellulase (composition chimique), Cellulase (isolement et purification), Cellulase (métabolisme), Cellulose (MeSH), Chromatographie d'échange d'ions (MeSH), Chromatographie sur gel (MeSH), Cinétique (MeSH), Données de séquences moléculaires (MeSH), Masse moléculaire (MeSH), Phanerochaete (génétique), Similitude de séquences d'acides aminés (MeSH).
- MESH :
- composition chimique : Cellulase.
- enzymologie : Basidiomycota.
- génétique : Phanerochaete.
- isolement et purification : Cellulase.
- métabolisme : Carboxyméthylcellulose de sodium, Cellobiose, Cellulase.
- Analyse de séquence de protéine, Cellulose, Chromatographie d'échange d'ions, Chromatographie sur gel, Cinétique, Données de séquences moléculaires, Masse moléculaire, Similitude de séquences d'acides aminés.
English descriptors
- KwdEn :
- Basidiomycota (enzymology), Carboxymethylcellulose Sodium (metabolism), Cellobiose (metabolism), Cellulase (chemistry), Cellulase (isolation & purification), Cellulase (metabolism), Cellulose (MeSH), Chromatography, Gel (MeSH), Chromatography, Ion Exchange (MeSH), Kinetics (MeSH), Molecular Sequence Data (MeSH), Molecular Weight (MeSH), Phanerochaete (genetics), Sequence Analysis, Protein (MeSH), Sequence Homology, Amino Acid (MeSH).
- MESH :
- chemical , chemistry : Cellulase.
- chemical , isolation & purification : Cellulase.
- chemical , metabolism : Carboxymethylcellulose Sodium, Cellobiose, Cellulase.
- enzymology : Basidiomycota.
- genetics : Phanerochaete.
- chemical : Cellulose, Chromatography, Gel, Chromatography, Ion Exchange, Kinetics, Molecular Sequence Data, Molecular Weight, Sequence Analysis, Protein, Sequence Homology, Amino Acid.
Abstract
Two endoglucanases with processive cellulase activities, produced from Fomitopsis palustris grown on 2% microcrystalline cellulose (Avicel), were purified to homogeneity by anion-exchange and gel filtration column chromatography systems. SDS-PAGE analysis indicated that the molecular masses of the purified enzymes were 47 kDa and 35 kDa, respectively. The amino acid sequence analysis of the 47-kDa protein (EG47) showed a sequence similarity with fungal glycoside hydrolase family 5 endoglucanase from the white-rot fungus Phanerochaete chrysosporium. N-terminal and internal amino acid sequences of the 35-kDa protein (EG35), however, had no homology with any other glycosylhydrolases, although the enzyme had high specific activity against carboxymethyl cellulose, which is a typical substrate for endoglucanases. The initial rate of Avicel hydrolysis by EG35 was relatively fast for 48 h, and the amount of soluble reducing sugar released after 96 h was 100 microg/ml. Although EG47 also hydrolyzed Avicel, the hydrolysis rate was lower than that of EG35. Thin layer chromatography analysis of the hydrolysis products released from Avicel indicated that the main product was cellobiose, suggesting that the brown-rot fungus possesses processive EGs capable of degrading crystalline cellulose.
PubMed: 18051302
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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<affiliation wicri:level="1"><nlm:affiliation>Department ofBioscience and Biotechnology, Konkuk University, Seoul 143-701, Korea. jjyoon@konkuk.ac.kr</nlm:affiliation>
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<wicri:regionArea>Department ofBioscience and Biotechnology, Konkuk University, Seoul 143-701</wicri:regionArea>
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<author><name sortKey="Kim, Yeong Suk" sort="Kim, Yeong Suk" uniqKey="Kim Y" first="Yeong-Suk" last="Kim">Yeong-Suk Kim</name>
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<author><name sortKey="Son, Dong Won" sort="Son, Dong Won" uniqKey="Son D" first="Dong-Won" last="Son">Dong-Won Son</name>
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<term>Cellulase (chemistry)</term>
<term>Cellulase (isolation & purification)</term>
<term>Cellulase (metabolism)</term>
<term>Cellulose (MeSH)</term>
<term>Chromatography, Gel (MeSH)</term>
<term>Chromatography, Ion Exchange (MeSH)</term>
<term>Kinetics (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Molecular Weight (MeSH)</term>
<term>Phanerochaete (genetics)</term>
<term>Sequence Analysis, Protein (MeSH)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Analyse de séquence de protéine (MeSH)</term>
<term>Basidiomycota (enzymologie)</term>
<term>Carboxyméthylcellulose de sodium (métabolisme)</term>
<term>Cellobiose (métabolisme)</term>
<term>Cellulase (composition chimique)</term>
<term>Cellulase (isolement et purification)</term>
<term>Cellulase (métabolisme)</term>
<term>Cellulose (MeSH)</term>
<term>Chromatographie d'échange d'ions (MeSH)</term>
<term>Chromatographie sur gel (MeSH)</term>
<term>Cinétique (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Masse moléculaire (MeSH)</term>
<term>Phanerochaete (génétique)</term>
<term>Similitude de séquences d'acides aminés (MeSH)</term>
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<term>Cellobiose</term>
<term>Cellulase</term>
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<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cellulase</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Carboxyméthylcellulose de sodium</term>
<term>Cellobiose</term>
<term>Cellulase</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Cellulose</term>
<term>Chromatography, Gel</term>
<term>Chromatography, Ion Exchange</term>
<term>Kinetics</term>
<term>Molecular Sequence Data</term>
<term>Molecular Weight</term>
<term>Sequence Analysis, Protein</term>
<term>Sequence Homology, Amino Acid</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Analyse de séquence de protéine</term>
<term>Cellulose</term>
<term>Chromatographie d'échange d'ions</term>
<term>Chromatographie sur gel</term>
<term>Cinétique</term>
<term>Données de séquences moléculaires</term>
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<front><div type="abstract" xml:lang="en">Two endoglucanases with processive cellulase activities, produced from Fomitopsis palustris grown on 2% microcrystalline cellulose (Avicel), were purified to homogeneity by anion-exchange and gel filtration column chromatography systems. SDS-PAGE analysis indicated that the molecular masses of the purified enzymes were 47 kDa and 35 kDa, respectively. The amino acid sequence analysis of the 47-kDa protein (EG47) showed a sequence similarity with fungal glycoside hydrolase family 5 endoglucanase from the white-rot fungus Phanerochaete chrysosporium. N-terminal and internal amino acid sequences of the 35-kDa protein (EG35), however, had no homology with any other glycosylhydrolases, although the enzyme had high specific activity against carboxymethyl cellulose, which is a typical substrate for endoglucanases. The initial rate of Avicel hydrolysis by EG35 was relatively fast for 48 h, and the amount of soluble reducing sugar released after 96 h was 100 microg/ml. Although EG47 also hydrolyzed Avicel, the hydrolysis rate was lower than that of EG35. Thin layer chromatography analysis of the hydrolysis products released from Avicel indicated that the main product was cellobiose, suggesting that the brown-rot fungus possesses processive EGs capable of degrading crystalline cellulose.</div>
</front>
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<Title>Journal of microbiology and biotechnology</Title>
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<ArticleTitle>The brown-rot basidiomycete Fomitopsis palustris has the endo-glucanases capable of degrading microcrystalline cellulose.</ArticleTitle>
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</Pagination>
<Abstract><AbstractText>Two endoglucanases with processive cellulase activities, produced from Fomitopsis palustris grown on 2% microcrystalline cellulose (Avicel), were purified to homogeneity by anion-exchange and gel filtration column chromatography systems. SDS-PAGE analysis indicated that the molecular masses of the purified enzymes were 47 kDa and 35 kDa, respectively. The amino acid sequence analysis of the 47-kDa protein (EG47) showed a sequence similarity with fungal glycoside hydrolase family 5 endoglucanase from the white-rot fungus Phanerochaete chrysosporium. N-terminal and internal amino acid sequences of the 35-kDa protein (EG35), however, had no homology with any other glycosylhydrolases, although the enzyme had high specific activity against carboxymethyl cellulose, which is a typical substrate for endoglucanases. The initial rate of Avicel hydrolysis by EG35 was relatively fast for 48 h, and the amount of soluble reducing sugar released after 96 h was 100 microg/ml. Although EG47 also hydrolyzed Avicel, the hydrolysis rate was lower than that of EG35. Thin layer chromatography analysis of the hydrolysis products released from Avicel indicated that the main product was cellobiose, suggesting that the brown-rot fungus possesses processive EGs capable of degrading crystalline cellulose.</AbstractText>
</Abstract>
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<country name="Corée du Sud"><region name="Région capitale de Séoul"><name sortKey="Yoon, Jeong Jun" sort="Yoon, Jeong Jun" uniqKey="Yoon J" first="Jeong-Jun" last="Yoon">Jeong-Jun Yoon</name>
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