Expression and secretion of barley cysteine endopeptidase B and cellobiohydrolase I in Trichoderma reesei

Article Abstract:

A research was conducted to investigate the localization of secretion and expression of a heterologous barley cysteine endopeptidase and the homologous main celobiohydrolase I in the filementous fungus Trichoderma reesei which expressed both proteins. A TRIzol reagent was utilized to isolate total RNA from the mycelia of T. reesei. Results showed that the recombinant cysteine proteinase was located in the hyphae at the colony edges. The hyphae accommodated several nuclei and a certain distance was always observed between the tip and the nucleus closest to it.

Bacterial transformation, Hydrolysis, Cysteine

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Expression of barley endopeptidase B in Trichoderma reesei

Article Abstract:

A research was conducted to investigate the expression of barley endopeptidase B (EPB) in Trichoderma reesei. Southern blotting was utilized to analyze the organization of the cbh1 locus in the transformed strains. DNAs were digested with XhoI and hybridized with the XbaI-SacII fragment of pALK584 to determine the numbers of copies of the EPB expression cassette. Moreover, a protein was detected in extracts of Asperigillus oryzae transformants which expressed recombinant thaumatin.

Genetic aspects, Fungi, Barley

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High yield production of a bacterial xylanase in the filamentous fungus Trichoderma reesei requires a carrier polypeptide with an intact domain structure

Article Abstract:

The gene fusion strategy was used to increase production of a bacterial enzyme from Trichoderma reesei. The conclusion states that the bacterial Xyn11A produced in T. reesei appeared to be correctly cleaved and had properties similar to those of the xylanase in N. flexuosa culture medium.

Science & research, Polypeptides, Gene fusion

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