Purification and characterization of an extracellular beta-glucosidase produced by Phoma sp. KCTC11825BP isolated from rotten mandarin peel.
Identifieur interne : 000745 ( PubMed/Corpus ); précédent : 000744; suivant : 000746Purification and characterization of an extracellular beta-glucosidase produced by Phoma sp. KCTC11825BP isolated from rotten mandarin peel.
Auteurs : Jung-Youn Choi ; 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
Links to Exploration step
pubmed:21617347Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><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><nlm:affiliation>Eco Technology Center, Chungcheong Regional Division, Korea Institute of Industrial Technology, Cheonan, Chungnam, Republic of Korea.</nlm:affiliation></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></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><nlm:affiliation>Eco Technology Center, Chungcheong Regional Division, Korea Institute of Industrial Technology, Cheonan, Chungnam, Republic of Korea.</nlm:affiliation></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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21617347</PMID><DateCreated><Year>2011</Year><Month>5</Month><Day>27</Day></DateCreated><DateCompleted><Year>2011</Year><Month>09</Month><Day>06</Day></DateCompleted><DateRevised><Year>2011</Year><Month>5</Month><Day>27</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1738-8872</ISSN><JournalIssue CitedMedium="Internet"><Volume>21</Volume><Issue>5</Issue><PubDate><Year>2011</Year><Month>May</Month></PubDate></JournalIssue><Title>Journal of microbiology and biotechnology</Title><ISOAbbreviation>J. Microbiol. Biotechnol.</ISOAbbreviation></Journal><ArticleTitle>Purification and characterization of an extracellular beta-glucosidase produced by Phoma sp. KCTC11825BP isolated from rotten mandarin peel.</ArticleTitle><Pagination><MedlinePgn>503-8</MedlinePgn></Pagination><Abstract><AbstractText>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+.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Choi</LastName><ForeName>Jung-Youn</ForeName><Initials>JY</Initials><AffiliationInfo><Affiliation>Eco Technology Center, Chungcheong Regional Division, Korea Institute of Industrial Technology, Cheonan, Chungnam, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Park</LastName><ForeName>Ah-Reum</ForeName><Initials>AR</Initials></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Yong Jin</ForeName><Initials>YJ</Initials></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Jae-Jin</ForeName><Initials>JJ</Initials></Author><Author ValidYN="Y"><LastName>Cha</LastName><ForeName>Chang-Jun</ForeName><Initials>CJ</Initials></Author><Author ValidYN="Y"><LastName>Yoon</LastName><ForeName>Jeong-Jun</ForeName><Initials>JJ</Initials></Author></AuthorList><Language>ENG</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Korea (South)</Country><MedlineTA>J Microbiol Biotechnol</MedlineTA><NlmUniqueID>9431852</NlmUniqueID><ISSNLinking>1017-7825</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.21</RegistryNumber><NameOfSubstance UI="D001617">beta-Glucosidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001203" MajorTopicYN="N">Ascomycota</DescriptorName><QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032084" MajorTopicYN="N">Citrus sinensis</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001617" MajorTopicYN="N">beta-Glucosidase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>5</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>5</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2011</Year><Month>9</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">21617347</ArticleId><ArticleId IdType="pii">JMB021-05-08</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Bois/explor/OrangerV1/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000745 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 000745 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Bois
|area= OrangerV1
|flux= PubMed
|étape= Corpus
|type= RBID
|clé= pubmed:21617347
|texte= Purification and characterization of an extracellular beta-glucosidase produced by Phoma sp. KCTC11825BP isolated from rotten mandarin peel.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:21617347" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a OrangerV1
| This area was generated with Dilib version V0.6.25. |  |