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Diethard Mattanovich

Researcher at University of Natural Resources and Life Sciences, Vienna

Publications -  250
Citations -  13462

Diethard Mattanovich is an academic researcher from University of Natural Resources and Life Sciences, Vienna. The author has contributed to research in topics: Pichia pastoris & Gene. The author has an hindex of 64, co-authored 241 publications receiving 11737 citations. Previous affiliations of Diethard Mattanovich include University of Agricultural Sciences, Dharwad & University of Agriculture, Faisalabad.

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Journal ArticleDOI

Microbial production of organic acids: expanding the markets.

TL;DR: Through analysis of the current advances in production of citric, lactic and succinic acid production, guidelines for future developments in this fast-moving field are presented.
Journal ArticleDOI

Adaptive laboratory evolution – principles and applications for biotechnology

TL;DR: The current status and its future perspectives highlight the importance and potential of adaptive laboratory evolution as approach in biotechnological engineering.
Book ChapterDOI

Recombinant Protein Production in Yeasts

TL;DR: Advantages and limitations of the main and most promising yeast hosts, including Saccharomyces cerevisiae, Pichia pastoris, and Hansenula polymorpha as those presently used in large scale production of heterologous proteins are summarized.
Journal ArticleDOI

Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview

TL;DR: In this article, the main cellular players of this complex process are described for the most important cell factories used for biotechnological purposes, and the characterization of such adverse conditions and the elicited cell responses have permitted to better understand the physiology and molecular biology of conformational stress.
Journal ArticleDOI

Effects of gene dosage, promoters, and substrates on unfolded protein stress of recombinant Pichia pastoris.

TL;DR: An increase of BiP was observed upon induction of expression, indicating that the intracellular product fraction exerts an unfolded protein response in the host cells.