Expression and processing of a major xylanase (XYN2) from the thermophilic fungus Humicola grisea var. thermoidea in Trichoderma reesei.

Autor: de Faria FP; Departamento de Biotecnologia, FAENQUIL, Lorena-SP, Brazil., Te'O VS, Bergquist PL, Azevedo MO, Nevalainen KM
Jazyk: angličtina
Zdroj: Letters in applied microbiology [Lett Appl Microbiol] 2002; Vol. 34 (2), pp. 119-23.
DOI: 10.1046/j.1472-765x.2002.01057.x
Abstrakt: Aims: To express a gene encoding a heterologous fungal xylanase in Trichoderma reesei.
Methods and Results: Humicola grisea xylanase 2 (xyn2) cDNA was expressed in Trichoderma reesei under the main cellobiohydrolase I (cbh1) promoter (i) as a fusion to the cellobiohydrolase I (CBHI) secretion signal and (ii) the mature CBHI core-linker. The recombinant xylanase (HXYN2) was secreted into the cultivation medium and processed in a similar fashion to the endogenous T. reesei xylanases, resulting in an active enzyme.
Conclusions, Significance and Impact of the Study: HXYN2 was successfully processed in T. reesei. Composition of the culture medium affected the HXYN2 yields, favouring Avicel-lactose as a carbon source. Best yields (about 0.5 g l(-1)) in shake flask cultivations were obtained from a transformant where xyn2 was fused directly to the CBHI secretion signal.
Databáze: MEDLINE
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