Barbara Petschacher
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Explore the profile of Barbara Petschacher including associated specialties, affiliations and a list of published articles.
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12
Citations
223
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Recent Articles
1.
Schelch S, Eibinger M, Gross Belduma S, Petschacher B, Kuballa J, Nidetzky B
Biotechnol Bioeng
. 2021 Jul;
118(11):4290-4304.
PMID: 34289079
Sialo-oligosaccharides are important products of emerging biotechnology for complex carbohydrates as nutritional ingredients. Cascade bio-catalysis is central to the development of sialo-oligosaccharide production systems, based on isolated enzymes or whole...
2.
Schelch S, Zhong C, Petschacher B, Nidetzky B
Biotechnol Adv
. 2020 Aug;
44:107613.
PMID: 32822768
Sialic acids are important recognition sites in protein- and lipid-linked glycans of higher organisms and of select bacteria and protozoa. They are also prominent in human milk oligosaccharides. Defined sialo-oligosaccharides...
3.
Petschacher B, Nidetzky B
J Biotechnol
. 2016 Apr;
235:61-83.
PMID: 27046065
Human milk oligosaccharides (HMOs) constitute a class of complex carbohydrates unique to mother's milk and are strongly correlated to the health benefits of breastfeeding in infants. HMOs are important as...
4.
Petschacher B, Staunig N, Muller M, Schurmann M, Mink D, De Wildeman S, et al.
Comput Struct Biotechnol J
. 2014 Apr;
9:e201402005.
PMID: 24757503
Soluble water-forming NAD(P)H oxidases constitute a promising NAD(P)(+) regeneration method as they only need oxygen as cosubstrate and produce water as sole byproduct. Moreover, the thermodynamic equilibrium of O2 reduction...
5.
Wilding B, Winkler M, Petschacher B, Kratzer R, Egger S, Steinkellner G, et al.
Chemistry
. 2013 Apr;
19(22):7007-12.
PMID: 23595998
Nitrile reductase QueF catalyzes the reduction of 2-amino-5-cyanopyrrolo[2,3-d]pyrimidin-4-one (preQ0) to 2-amino-5-aminomethylpyrrolo[2,3-d]pyrimidin-4-one (preQ1) in the biosynthetic pathway of the hypermodified nucleoside queuosine. It is the only enzyme known to catalyze a...
6.
Krahulec S, Petschacher B, Wallner M, Longus K, Klimacek M, Nidetzky B
Microb Cell Fact
. 2010 Mar;
9:16.
PMID: 20219100
Background: In spite of the substantial metabolic engineering effort previously devoted to the development of Saccharomyces cerevisiae strains capable of fermenting both the hexose and pentose sugars present in lignocellulose...
7.
Petschacher B, Nidetzky B
Microb Cell Fact
. 2008 Mar;
7:9.
PMID: 18346277
Background: Metabolic engineering of Saccharomyces cerevisiae for xylose fermentation into fuel ethanol has oftentimes relied on insertion of a heterologous pathway that consists of xylose reductase (XR) and xylitol dehydrogenase...
8.
di Luccio E, Petschacher B, Voegtli J, Chou H, Stahlberg H, Nidetzky B, et al.
J Mol Biol
. 2006 Nov;
365(3):783-98.
PMID: 17123542
The primary metabolic route for D-xylose, the second most abundant sugar in nature, is via the pentose phosphate pathway after a two-step or three-step conversion to xylulose-5-phosphate. Xylulose kinase (XK;...
9.
Petschacher B, Nidetzky B
Appl Environ Microbiol
. 2005 Oct;
71(10):6390-3.
PMID: 16204564
Six single- and multiple-site variants of Candida tenuis xylose reductase that were engineered to have side chain replacements in the coenzyme 2'-phosphate binding pocket were tested for NADPH versus NADH...
10.
Leitgeb S, Petschacher B, Wilson D, Nidetzky B
FEBS Lett
. 2005 Jan;
579(3):763-7.
PMID: 15670843
Aldo-keto reductases of family 2 employ single site replacement Lys-->Arg to switch their cosubstrate preference from NADPH to NADH. X-ray crystal structures of Lys-274-->Arg mutant of Candida tenuis xylose reductase...