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Doris Hartinger
BIOMIN Research Center, Technopark 1, 3430 Tulln, Austria

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Journal article
Published: 20 August 2019 in Toxins
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Zearalenone (ZEN)-degrading enzymes are a promising strategy to counteract the negative effects of this mycotoxin in livestock. The reaction products of such enzymes need to be thoroughly characterized before technological application as a feed additive can be envisaged. Here, we evaluated the estrogenic activity of the metabolites hydrolyzed zearalenone (HZEN) and decarboxylated hydrolyzed zearalenone (DHZEN) formed by hydrolysis of ZEN by the zearalenone-lactonase Zhd101p. ZEN, HZEN, and DHZEN were tested in two in vitro models, the MCF-7 cell proliferation assay (0.01-500 nM) and an estrogen-sensitive yeast bioassay (1-10,000 nM). In addition, we compared the impact of dietary ZEN (4.58 mg/kg) and equimolar dietary concentrations of HZEN and DHZEN on reproductive tract morphology as well as uterine mRNA and microRNA expression in female piglets (n = 6, four weeks exposure). While ZEN increased cell proliferation and reporter gene transcription, neither HZEN nor DHZEN elicited an estrogenic response, suggesting that these metabolites are at least 50-10,000 times less estrogenic than ZEN in vitro. In piglets, HZEN and DHZEN did not increase vulva size or uterus weight. Moreover, RNA transcripts altered upon ZEN treatment (EBAG9, miR-135a-5p, miR-187-3p and miR-204-5p) were unaffected by HZEN and DHZEN. Our study shows that both metabolites exhibit markedly reduced estrogenicity in vitro and in vivo, and thus provides an important basis for further evaluation of ZEN-degrading enzymes.

ACS Style

Sebastian Fruhauf; Barbara Novak; Veronika Nagl; Matthias Hackl; Doris Hartinger; Valentina Rainer; Silvia Labudová; Gerhard Adam; Markus Aleschko; Wulf-Dieter Moll; Michaela Thamhesl; Bertrand Grenier. Biotransformation of the Mycotoxin Zearalenone to its Metabolites Hydrolyzed Zearalenone (HZEN) and Decarboxylated Hydrolyzed Zearalenone (DHZEN) Diminishes its Estrogenicity In Vitro and In Vivo. Toxins 2019, 11, 481 .

AMA Style

Sebastian Fruhauf, Barbara Novak, Veronika Nagl, Matthias Hackl, Doris Hartinger, Valentina Rainer, Silvia Labudová, Gerhard Adam, Markus Aleschko, Wulf-Dieter Moll, Michaela Thamhesl, Bertrand Grenier. Biotransformation of the Mycotoxin Zearalenone to its Metabolites Hydrolyzed Zearalenone (HZEN) and Decarboxylated Hydrolyzed Zearalenone (DHZEN) Diminishes its Estrogenicity In Vitro and In Vivo. Toxins. 2019; 11 (8):481.

Chicago/Turabian Style

Sebastian Fruhauf; Barbara Novak; Veronika Nagl; Matthias Hackl; Doris Hartinger; Valentina Rainer; Silvia Labudová; Gerhard Adam; Markus Aleschko; Wulf-Dieter Moll; Michaela Thamhesl; Bertrand Grenier. 2019. "Biotransformation of the Mycotoxin Zearalenone to its Metabolites Hydrolyzed Zearalenone (HZEN) and Decarboxylated Hydrolyzed Zearalenone (DHZEN) Diminishes its Estrogenicity In Vitro and In Vivo." Toxins 11, no. 8: 481.

Journal article
Published: 01 January 2010 in Microbial Cell Factories
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Fumonisin B1 is a cancerogenic mycotoxin produced by Fusarium verticillioides and other fungi. Sphingopyxis sp. MTA144 can degrade fumonisin B1, and a key enzyme in the catabolic pathway is an aminotransferase which removes the C2-amino group from hydrolyzed fumonisin B1. In order to study this aminotransferase with respect to a possible future application in enzymatic fumonisin detoxification, we attempted expression of the corresponding fumI gene in E. coli and purification of the enzyme. Since the aminotransferase initially accumulated in inclusion bodies, we compared the effects of induction level, host strain, expression temperature, solubility enhancers and a fusion partner on enzyme solubility and activity.

ACS Style

Doris Hartinger; Stefan Heinl; Heidi Elisabeth Schwartz; Reingard Grabherr; Gerd Schatzmayr; Dietmar Haltrich; Wulf-Dieter Moll. Enhancement of solubility in Escherichia coli and purification of an aminotransferase from Sphingopyxis sp. MTA144 for deamination of hydrolyzed fumonisin B1. Microbial Cell Factories 2010, 9, 62 -14.

AMA Style

Doris Hartinger, Stefan Heinl, Heidi Elisabeth Schwartz, Reingard Grabherr, Gerd Schatzmayr, Dietmar Haltrich, Wulf-Dieter Moll. Enhancement of solubility in Escherichia coli and purification of an aminotransferase from Sphingopyxis sp. MTA144 for deamination of hydrolyzed fumonisin B1. Microbial Cell Factories. 2010; 9 (1):62-14.

Chicago/Turabian Style

Doris Hartinger; Stefan Heinl; Heidi Elisabeth Schwartz; Reingard Grabherr; Gerd Schatzmayr; Dietmar Haltrich; Wulf-Dieter Moll. 2010. "Enhancement of solubility in Escherichia coli and purification of an aminotransferase from Sphingopyxis sp. MTA144 for deamination of hydrolyzed fumonisin B1." Microbial Cell Factories 9, no. 1: 62-14.