Bibliographic Details
| Title: |
Characterization of the catalytic domains of Trichoderma reesei endoglucanase I, II, and III, expressed in Escherichia coli. |
| Authors: |
Nakazawa, Hikaru1, Okada, Katsunori1, Kobayashi, Ryota1, Kubota, Tetsuya1, Onodera, Tomoko1, Ochiai, Nobuhiro1, Omata, Naoki1, Ogasawara, Wataru1, Okada, Hirofumi1, Morikawa, Yasushi1 yasushi@vos.nagaokaut.ac.jp |
| Superior Title: |
Applied Microbiology & Biotechnology. Dec2008, Vol. 81 Issue 4, p681-689. 9p. 2 Black and White Photographs, 4 Charts, 3 Graphs. |
| Subject Terms: |
*TRICHODERMA reesei, *ESCHERICHIA coli, *CATALYSIS, *CELLULOSE, *PROTEINS, *LOW temperatures, *GLUCANS |
| Abstract: |
The genes encoding the catalytic domains (CD) of the three endoglucanases (EG I; Cel7B, EG II; Cel5A, and EG III; Cel12A) from Trichoderma reesei QM9414 were expressed in Escherichia coli strains Rosetta-gami B (DE3) pLacI or Origami B (DE3) pLacI and were found to produce functional intracellular proteins. Protein production by the three endoglucanase transformants was evaluated as a function of growth temperature. Maximal productivity of EG I-CD at 15°C, EG II-CD at 20°C and EG III at 37°C resulted in yields of 6.9, 72, and 50 mg/l, respectively. The endoglucanases were purified using a simple purification method based on removing E. coli proteins by isoelectric point precipitation. Specific activity toward carboxymethyl cellulose was found to be 65, 49, and 15 U/mg for EG I-CD, EG II-CD, and EG III, respectively. EG II-CD was able to cleave 1,3–1,4-β- d-glucan and soluble cellulose derivatives. EG III was found to be active against cellulose, 1,3–1,4-β- d-glucan and xyloglucan, while EG I-CD was active against cellulose, 1,3–1,4-β- d-glucan, xyloglucan, xylan, and mannan. [ABSTRACT FROM AUTHOR] |
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| Database: |
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