TY - JOUR A1 - Eilert, Eva A1 - Kranz, Andreas A1 - Hollenberg, Cornelis P. A1 - Piontek, Michael A1 - Suckow, Manfred T1 - Synthesis and release of the bacterial compatible solute 5-hydroxyectoine in Hansenula polymorpha JF - Journal of biotechnology N2 - Ectoine and 5-hydroxyectoine belong to the family of compatible solutes which are known to mainly contribute to the adaptation of the cell to osmotic stress by mediation of a constant turgor. In addition the cell's essential functions are maintained under stress conditions like high salinity, heat or aridity stress. Hansenula polymorpha was engineered to catalyze the transformation of monomeric substrates to 5-hydroxyectoine. For this purpose four genes encoding the enzymes of the 5-hydroxyectoine biosynthesis pathway of Halomonas elongata, EctA, EctB, EctC, and EctD, were inserted into the genome of H. polymorpha. Subsequently the syntheses of ectoine and 5-hydroxyectoine were analyzed and optimized. We showed that H. polymorpha is a suitable system for recombinant 5-hydroxyectoine synthesis in gram per liter scale (2.8 g L⁻¹ culture supernatant, 365 μmol/g dcw) in which almost 100% conversion of ectoine to 5-hydroxyectoine without necessity of high salinity were achieved. Y1 - 2013 UR - http://www.ncbi.nlm.nih.gov/pubmed/23467000 U6 - https://doi.org/10.1016/j.jbiotec.2013.02.005 VL - 167 IS - 2 SP - 85 EP - 93 PB - Elsevier ER - TY - JOUR A1 - Eilert, Eva A1 - Hollenberg, Cornelis P. A1 - Piontek, Michael A1 - Suckow, Manfred T1 - The use of highly expressed FTH1 as carrier protein for cytosolic targeting in Hansenula polymorpha JF - Journal of biotechnology N2 - The iron storage protein ferritin is a member of the non-heme iron protein family. It can store and release iron, therefore it prevents the cell from damage caused by iron-dioxygen reactions as well as it provides iron for biological processing. To study whether the human ferritin heavy chain (FTH1) can be expressed in Hansenula polymorpha, we integrated an expression cassette for FTH1 and analyzed the protein expression. We found very efficient expression of FTH1 and obtained yields up to 1.9 g/L under non-optimized conditions. Based on this result we designed a FTH1-PTH fusion protein to successfully express the parathyroid hormone fragment 1-34 (PTH) for the first time intracellular in H. polymorpha. Y1 - 2012 UR - http://www.ncbi.nlm.nih.gov/pubmed/22212821 U6 - https://doi.org/10.1016/j.jbiotec.2011.12.014 VL - 159 IS - 3 SP - 172 EP - 176 PB - Elsevier ER - TY - PAT A1 - Kraemer, Marco A1 - Svetlichny, Vitaly A1 - Eilert, Eva T1 - Method for producing a fermentation product: Angemeldet durch DIREVO Industrial Biotechnology GmbH N2 - Prioritätsdaten: EP15191039A·2015-10-22; US201562245054P·2015-10-22 Bibliographische IPC: C12P7/06; C12P7/14; Y1 - 2017 UR - https://depatisnet.dpma.de/DepatisNet/depatisnet?action=pdf&docid=WO002017067698A1&xxxfull=1 ER - TY - PAT A1 - Eilert, Eva A1 - Suckow, Manfred A1 - Piontek, Michael T1 - A method for producing ectoine or a derivative thereof and a yeast cell for use as a host cell in such a method N2 - Klassifikationen IPC C12N15/81; C12N15/82; C12P17/12; C12P7/42; CPC C12N15/815 (EP); C12P17/12 (EP); Y1 - 2014 UR - https://depatisnet.dpma.de/DepatisNet/depatisnet?action=pdf&docid=EP000002743350A1&xxxfull=1 ER -