In-fusion expression and characterization of β-xylanase and β-1,3-1,4-glucanase in Pichia pastoris
Abstract: Two chimeric genes, XynA-Bs-Glu-1 and XynA-Bs-Glu-2, encoding Aspergillus sulphureus β-xylanase (XynA, 26 kDa) and Bacillus subtilis β-1,3-1,4-glucanase (Bs-Glu, 30 kDa), were constructed via in-fusion by different linkers and expressed successfully in Pichia pastoris. The fusion protein (50 kDa) exhibited both β-xylanase and β-1,3-1,4-glucanase activities. Compared with parental enzymes, the moiety activities were decreased in fermentation supernatants. Parental XynA and Bs-Glu were superior to corresponding moieties in each fusion enzymes because of lower Kn higher kcat. Despite some variations, common optima were generally 50°C and pH 3.4 for the XynA moiety and parent, and 40°C and pH 6.4 for the Bs-Glu counterparts. Thus, the fusion enzyme XynA-Bs-Glu-1 and XynA-Bs-Glu-2 were bifunctional.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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In-fusion expression and characterization of β-xylanase and β-1,3-1,4-glucanase in Pichia pastoris ; volume:67 ; number:4 ; year:2012 ; pages:649-653 ; extent:5
Biologia ; 67, Heft 4 (2012), 649-653 (gesamt 5)
- Creator
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Qiao, Jiayun
Cao, Yunhe
- DOI
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10.2478/s11756-012-0056-3
- URN
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urn:nbn:de:101:1-2409221734184.580549594968
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:37 AM CEST
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Associated
- Qiao, Jiayun
- Cao, Yunhe
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