Construction of the bifunctional enzyme cellulase-b-glucosidase from the hyperthermophilic bacterium Thermotoga maritima
An artificial bifunctional enzyme, cellulase-b-glucosidase, was prepared by gene fusion from the hyperthermophilic bacterium Thermotoga maritima MSB8. The fusion protein exhibited both cellulase (Cel5C) and b-glucosidase (BglB) activity when the bglB gene was fused to downstream of cel5C, but not wh...
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| Veröffentlicht in: | Biotechnology letters 2007-06, Vol.29 (6), p.931-936 |
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| container_title | Biotechnology letters |
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| creator | Hong, Su-Young Lee, Jin-Suk Cho, Kye-Man Math, Renukaradhya K Kim, Yong-Hee Hong, Sun-Joo Cho, Yong-Un Cho, Soo-Jeong Kim, Hoon Yun, Han-Dae |
| description | An artificial bifunctional enzyme, cellulase-b-glucosidase, was prepared by gene fusion from the hyperthermophilic bacterium Thermotoga maritima MSB8. The fusion protein exhibited both cellulase (Cel5C) and b-glucosidase (BglB) activity when the bglB gene was fused to downstream of cel5C, but not when cel5C was fused to downstream of bglB. The specific activity of the bifunctional enzyme was 70% lower than that of cellulase or b-glucosidase. The fusion enzyme was purified, and the MW was estimated as 114 kDa. The fusion enzyme displayed optimum cellulase activity at pH 8.0 and 70C over 30 min, and optimal b-glucosidase activity at pH 7.0 and 80C over 30 min. |
| doi_str_mv | 10.1007/s10529-007-9334-5 |
| format | Article |
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The fusion protein exhibited both cellulase (Cel5C) and b-glucosidase (BglB) activity when the bglB gene was fused to downstream of cel5C, but not when cel5C was fused to downstream of bglB. The specific activity of the bifunctional enzyme was 70% lower than that of cellulase or b-glucosidase. The fusion enzyme was purified, and the MW was estimated as 114 kDa. The fusion enzyme displayed optimum cellulase activity at pH 8.0 and 70C over 30 min, and optimal b-glucosidase activity at pH 7.0 and 80C over 30 min.</description><identifier>ISSN: 0141-5492</identifier><identifier>DOI: 10.1007/s10529-007-9334-5</identifier><language>eng</language><subject>Bacteria ; Thermotoga maritima</subject><ispartof>Biotechnology letters, 2007-06, Vol.29 (6), p.931-936</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Hong, Su-Young</creatorcontrib><creatorcontrib>Lee, Jin-Suk</creatorcontrib><creatorcontrib>Cho, Kye-Man</creatorcontrib><creatorcontrib>Math, Renukaradhya K</creatorcontrib><creatorcontrib>Kim, Yong-Hee</creatorcontrib><creatorcontrib>Hong, Sun-Joo</creatorcontrib><creatorcontrib>Cho, Yong-Un</creatorcontrib><creatorcontrib>Cho, Soo-Jeong</creatorcontrib><creatorcontrib>Kim, Hoon</creatorcontrib><creatorcontrib>Yun, Han-Dae</creatorcontrib><title>Construction of the bifunctional enzyme cellulase-b-glucosidase from the hyperthermophilic bacterium Thermotoga maritima</title><title>Biotechnology letters</title><description>An artificial bifunctional enzyme, cellulase-b-glucosidase, was prepared by gene fusion from the hyperthermophilic bacterium Thermotoga maritima MSB8. 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| ispartof | Biotechnology letters, 2007-06, Vol.29 (6), p.931-936 |
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| subjects | Bacteria Thermotoga maritima |
| title | Construction of the bifunctional enzyme cellulase-b-glucosidase from the hyperthermophilic bacterium Thermotoga maritima |
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