K
Katrin Greimel
Researcher at University of Natural Resources and Life Sciences, Vienna
Publications - 16
Citations - 944
Katrin Greimel is an academic researcher from University of Natural Resources and Life Sciences, Vienna. The author has contributed to research in topics: Cutinase & Alkyd. The author has an hindex of 10, co-authored 16 publications receiving 700 citations.
Papers
More filters
Journal ArticleDOI
Enzymatic surface hydrolysis of PET : effect of structural diversity on kinetic properties of cutinases from thermobifida
Enrique Herrero Acero,Doris Ribitsch,Georg Steinkellner,Karl Gruber,Katrin Greimel,Inge Eiteljoerg,Eva Trotscha,Ren Wei,Wolfgang Zimmermann,Manfred Zinn,Artur Cavaco-Paulo,Giuliano Freddi,Helmut Schwab,Georg M. Guebitz +13 more
TL;DR: Cutinases from Thermobifida cellulosilytica DSM44535 and fusca DSM44342 hydrolyzing poly(ethylene terephthalate) (PET) were successfully cloned and expressed in E.coli BL21-Gold(DE3).
Journal ArticleDOI
Hydrolysis of polyethyleneterephthalate by p-nitrobenzylesterase from Bacillus subtilis.
Doris Ribitsch,Sonja Heumann,Eva Trotscha,Enrique Herrero Acero,Katrin Greimel,Regina Leber,Ruth Birner-Gruenberger,Sigrid Deller,Inge Eiteljoerg,Peter Remler,Thomas Weber,Petra Siegert,Karl-Heinz Maurer,Ilaria Donelli,Giuliano Freddi,Helmut Schwab,Georg M. Guebitz +16 more
TL;DR: PET‐hydrolase active strains produced clearing zones and led to the release of the 3PET hydrolysis products terephthalic acid (TA), benzoic Acid (BA), 2‐Hydroxyethyl benzoate (HEB), and mono‐(2‐hydroxyethyl) terecularate (MHET) in 3PET supplemented liquid cultures.
Journal ArticleDOI
Fusion of binding domains to Thermobifida cellulosilytica cutinase to tune sorption characteristics and enhancing PET hydrolysis.
Doris Ribitsch,Antonio Orcal Yebra,Sabine Zitzenbacher,Jing Wu,Susanne Nowitsch,Georg Steinkellner,Katrin Greimel,Aleš Doliška,Gustav Oberdorfer,Christian Gruber,Karl Gruber,Helmut Schwab,Karin Stana-Kleinschek,Enrique Herrero Acero,Georg M. Guebitz +14 more
TL;DR: Increased adsorption to PET by the fusion enzymes was confirmed with Quarz Crystal Microbalance (QCM-D) analysis and indeed resulted in enhanced hydrolysis activity (3.8× for Thc_Cut1+CBM) on PET, as quantified, based on released mono/oligomers.
Journal ArticleDOI
A New Esterase from Thermobifida halotolerans Hydrolyses Polyethylene Terephthalate (PET) and Polylactic Acid (PLA)
Doris Ribitsch,Enrique Herrero Acero,Katrin Greimel,Anita Dellacher,Sabine Zitzenbacher,Annemarie Marold,Rosario Diaz Rodriguez,Georg Steinkellner,Karl Gruber,Helmut Schwab,Georg M. Guebitz +10 more
TL;DR: A new esterase from Thermobifida halotolerans (Thh_Est) was cloned and expressed in E. coli and investigated for surface hydrolysis of polylactic acid (PLA) and polyethylene terephthalate (PET) as discussed by the authors.
Journal ArticleDOI
Characterization of a new cutinase from Thermobifida alba for PET-surface hydrolysis
Doris Ribitsch,Enrique Herrero Acero,Katrin Greimel,Inge Eiteljoerg,Eva Trotscha,Giuliano Freddi,Helmut Schwab,Georg M. Guebitz +7 more
TL;DR: A new cutinase from Thermobifida alba (Tha_Cut1) was cloned and characterized for polyethylene terephthalate (PET) hydrolysis leading to considerable improvement in hydrophilicity quantified based on a decrease of the water contact angle.