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Robert L. Mach

Researcher at Vienna University of Technology

Publications -  17
Citations -  3343

Robert L. Mach is an academic researcher from Vienna University of Technology. The author has contributed to research in topics: Trichoderma reesei & Catabolite repression. The author has an hindex of 17, co-authored 17 publications receiving 3128 citations.

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Xyr1 (Xylanase Regulator 1) Regulates both the Hydrolytic Enzyme System and d-Xylose Metabolism in Hypocrea jecorina

TL;DR: Examination of the growth behavior of the different mutant strains of the H. jecorina genome pointed to the strongly reduced ability of the xyr1 deletion strain to utilize d-xylose and xylan, and transcriptional regulation of the major hydrolytic enzyme-encoding genes xyn1 and xyn2, cbh1 and cbh2, and egl1 (endoglucanase 1 and 2) is strictly dependent on Xyr1.
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Regulation of transcription of cellulases- and hemicellulases-encoding genes in Aspergillus niger and Hypocrea jecorina (Trichoderma reesei).

TL;DR: The similarities and differences in the transcriptional regulation of expression of hemicellulases and cellulases in A. niger and H. jecorina are described.
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Crel, the carbon catabolite repressor protein from Trichoderma reesei

TL;DR: It is concluded that T. reesei Cre1 is the functional homologue of Aspergillus CreA and that it binds to its target sequence probably as a protein complex.
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Bacterial diversity along a 2600 km river continuum

TL;DR: A comprehensive dataset detailing the bacterioplankton diversity along the midstream of the Danube River and its tributaries is presented, revealing that bacterial richness and evenness gradually declined downriver in both the free‐living and particle‐associated bacterial communities.
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The two major xylanases from Trichoderma reesei: characterization of both enzymes and genes.

TL;DR: As a first step to exploit the potential of Trichoderma reesei to produce hemicellulases, two endo-β-1,4-xylanases are purified and cloned and the enzyme encoded by xyn2 appears to more closely resemble several other bacterial and fungal xylanases than does that of xyn1.