Purification and characterization of an extracellular beta-glucosidase produced by Phoma sp. KCTC11825BP isolated from rotten mandarin peel.
Identifieur interne : 001662 ( Main/Exploration ); précédent : 001661; suivant : 001663Purification 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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Le document en format XML
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<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>
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<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>
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