Purification and characterization of an extracellular beta-glucosidase produced by Phoma sp. KCTC11825BP isolated from rotten mandarin peel.
Identifieur interne : 000D41 ( Ncbi/Checkpoint ); précédent : 000D40; suivant : 000D42Purification and characterization of an extracellular beta-glucosidase produced by Phoma sp. KCTC11825BP isolated from rotten mandarin peel.
Auteurs : Jung-Youn Choi [Corée du Sud] ; Ah-Reum Park ; Yong Jin Kim ; Jae-Jin Kim ; Chang-Jun Cha ; Jeong-Jun YoonSource :
- Journal of microbiology and biotechnology [ 1738-8872 ] ; 2011.
English descriptors
- KwdEn :
- Ascomycota (classification), Ascomycota (enzymology), Ascomycota (genetics), Ascomycota (isolation & purification), Citrus sinensis (chemistry), Citrus sinensis (microbiology), Enzyme Stability, Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (isolation & purification), Fungal Proteins (metabolism), Kinetics, Molecular Sequence Data, Molecular Weight, Phylogeny, Substrate Specificity, beta-Glucosidase (chemistry), beta-Glucosidase (genetics), beta-Glucosidase (isolation & purification), beta-Glucosidase (metabolism).
- MESH :
- chemical , chemistry : Fungal Proteins, beta-Glucosidase.
- chemistry : Citrus sinensis.
- classification : Ascomycota.
- enzymology : Ascomycota.
- genetics : Ascomycota, Fungal Proteins, beta-Glucosidase.
- isolation & purification : Ascomycota, Fungal Proteins, beta-Glucosidase.
- chemical , metabolism : Fungal Proteins, beta-Glucosidase.
- microbiology : Citrus sinensis.
- Enzyme Stability, Kinetics, Molecular Sequence Data, Molecular Weight, Phylogeny, Substrate Specificity.
Abstract
A beta-glucosidase from Phoma sp. KCTC11825BP isolated from rotten mandarin peel was purified 8.5-fold with a specific activity of 84.5 U/mg protein. The purified enzyme had a molecular mass of 440 kDa with a subunit of 110 kDa. The partial amino acid sequence of the purified beta-glucosidase evidenced high homology with the fungal beta- glucosidases belonging to glycosyl hydrolase family 3. Its optimal activity was detected at pH 4.5 and 60 degrees C, and the enzyme had a half-life of 53 h at 60 degrees C. The Km values for p-nitrophenyl-beta-D-glucopyranoside and cellobiose were 0.3 mM and 3.2 mM, respectively. The enzyme was competitively inhibited by both glucose (Ki=1.7 mM) and glucono-delta-lactone (Ki=0.1 mM) when pNPG was used as the substrate. Its activity was inhibited by 41% by 10 mM Cu2+ and stimulated by 20% by 10 mM Mg2+.
PubMed: 21617347
Affiliations:
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KCTC11825BP isolated from rotten mandarin peel.</title><author><name sortKey="Choi, Jung Youn" sort="Choi, Jung Youn" uniqKey="Choi J" first="Jung-Youn" last="Choi">Jung-Youn Choi</name><affiliation wicri:level="1"><nlm:affiliation>Eco Technology Center, Chungcheong Regional Division, Korea Institute of Industrial Technology, Cheonan, Chungnam, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Eco Technology Center, Chungcheong Regional Division, Korea Institute of Industrial Technology, Cheonan, Chungnam</wicri:regionArea><wicri:noRegion>Chungnam</wicri:noRegion></affiliation></author><author><name sortKey="Park, Ah Reum" sort="Park, Ah Reum" uniqKey="Park A" first="Ah-Reum" last="Park">Ah-Reum Park</name></author><author><name sortKey="Kim, Yong Jin" sort="Kim, Yong Jin" uniqKey="Kim Y" first="Yong Jin" last="Kim">Yong Jin Kim</name></author><author><name sortKey="Kim, Jae Jin" sort="Kim, Jae Jin" uniqKey="Kim J" first="Jae-Jin" last="Kim">Jae-Jin Kim</name></author><author><name sortKey="Cha, Chang Jun" sort="Cha, Chang Jun" uniqKey="Cha C" first="Chang-Jun" last="Cha">Chang-Jun Cha</name></author><author><name sortKey="Yoon, Jeong Jun" sort="Yoon, Jeong Jun" uniqKey="Yoon J" first="Jeong-Jun" last="Yoon">Jeong-Jun Yoon</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2011">2011</date><idno type="RBID">pubmed:21617347</idno><idno type="pmid">21617347</idno><idno type="wicri:Area/PubMed/Corpus">000745</idno><idno type="wicri:Area/PubMed/Curation">000745</idno><idno type="wicri:Area/PubMed/Checkpoint">000745</idno><idno type="wicri:Area/Ncbi/Merge">000D41</idno><idno type="wicri:Area/Ncbi/Curation">000D41</idno><idno type="wicri:Area/Ncbi/Checkpoint">000D41</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Purification and characterization of an extracellular beta-glucosidase produced by Phoma sp. KCTC11825BP isolated from rotten mandarin peel.</title><author><name sortKey="Choi, Jung Youn" sort="Choi, Jung Youn" uniqKey="Choi J" first="Jung-Youn" last="Choi">Jung-Youn Choi</name><affiliation wicri:level="1"><nlm:affiliation>Eco Technology Center, Chungcheong Regional Division, Korea Institute of Industrial Technology, Cheonan, Chungnam, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Eco Technology Center, Chungcheong Regional Division, Korea Institute of Industrial Technology, Cheonan, Chungnam</wicri:regionArea><wicri:noRegion>Chungnam</wicri:noRegion></affiliation></author><author><name sortKey="Park, Ah Reum" sort="Park, Ah Reum" uniqKey="Park A" first="Ah-Reum" last="Park">Ah-Reum Park</name></author><author><name sortKey="Kim, Yong Jin" sort="Kim, Yong Jin" uniqKey="Kim Y" first="Yong Jin" last="Kim">Yong Jin Kim</name></author><author><name sortKey="Kim, Jae Jin" sort="Kim, Jae Jin" uniqKey="Kim J" first="Jae-Jin" last="Kim">Jae-Jin Kim</name></author><author><name sortKey="Cha, Chang Jun" sort="Cha, Chang Jun" uniqKey="Cha C" first="Chang-Jun" last="Cha">Chang-Jun Cha</name></author><author><name sortKey="Yoon, Jeong Jun" sort="Yoon, Jeong Jun" uniqKey="Yoon J" first="Jeong-Jun" last="Yoon">Jeong-Jun Yoon</name></author></analytic><series><title level="j">Journal of microbiology and biotechnology</title><idno type="eISSN">1738-8872</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Ascomycota (classification)</term><term>Ascomycota (enzymology)</term><term>Ascomycota (genetics)</term><term>Ascomycota (isolation & purification)</term><term>Citrus sinensis (chemistry)</term><term>Citrus sinensis (microbiology)</term><term>Enzyme Stability</term><term>Fungal Proteins (chemistry)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (isolation & purification)</term><term>Fungal Proteins (metabolism)</term><term>Kinetics</term><term>Molecular Sequence Data</term><term>Molecular Weight</term><term>Phylogeny</term><term>Substrate Specificity</term><term>beta-Glucosidase (chemistry)</term><term>beta-Glucosidase (genetics)</term><term>beta-Glucosidase (isolation & purification)</term><term>beta-Glucosidase (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fungal Proteins</term><term>beta-Glucosidase</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Citrus sinensis</term></keywords><keywords scheme="MESH" qualifier="classification" xml:lang="en"><term>Ascomycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Ascomycota</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Ascomycota</term><term>Fungal Proteins</term><term>beta-Glucosidase</term></keywords><keywords scheme="MESH" qualifier="isolation & purification" xml:lang="en"><term>Ascomycota</term><term>Fungal Proteins</term><term>beta-Glucosidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term><term>beta-Glucosidase</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Citrus sinensis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Enzyme Stability</term><term>Kinetics</term><term>Molecular Sequence Data</term><term>Molecular Weight</term><term>Phylogeny</term><term>Substrate Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A beta-glucosidase from Phoma sp. KCTC11825BP isolated from rotten mandarin peel was purified 8.5-fold with a specific activity of 84.5 U/mg protein. The purified enzyme had a molecular mass of 440 kDa with a subunit of 110 kDa. The partial amino acid sequence of the purified beta-glucosidase evidenced high homology with the fungal beta- glucosidases belonging to glycosyl hydrolase family 3. Its optimal activity was detected at pH 4.5 and 60 degrees C, and the enzyme had a half-life of 53 h at 60 degrees C. The Km values for p-nitrophenyl-beta-D-glucopyranoside and cellobiose were 0.3 mM and 3.2 mM, respectively. The enzyme was competitively inhibited by both glucose (Ki=1.7 mM) and glucono-delta-lactone (Ki=0.1 mM) when pNPG was used as the substrate. Its activity was inhibited by 41% by 10 mM Cu2+ and stimulated by 20% by 10 mM Mg2+.</div></front></TEI><affiliations><list><country><li>Corée du Sud</li></country></list><tree><noCountry><name sortKey="Cha, Chang Jun" sort="Cha, Chang Jun" uniqKey="Cha C" first="Chang-Jun" last="Cha">Chang-Jun Cha</name><name sortKey="Kim, Jae Jin" sort="Kim, Jae Jin" uniqKey="Kim J" first="Jae-Jin" last="Kim">Jae-Jin Kim</name><name sortKey="Kim, Yong Jin" sort="Kim, Yong Jin" uniqKey="Kim Y" first="Yong Jin" last="Kim">Yong Jin Kim</name><name sortKey="Park, Ah Reum" sort="Park, Ah Reum" uniqKey="Park A" first="Ah-Reum" last="Park">Ah-Reum Park</name><name sortKey="Yoon, Jeong Jun" sort="Yoon, Jeong Jun" uniqKey="Yoon J" first="Jeong-Jun" last="Yoon">Jeong-Jun Yoon</name></noCountry><country name="Corée du Sud"><noRegion><name sortKey="Choi, Jung Youn" sort="Choi, Jung Youn" uniqKey="Choi J" first="Jung-Youn" last="Choi">Jung-Youn Choi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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