Dr. Peter Stockinger
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Dr. Peter Stockinger
ZHAW
Life Sciences und Facility Management
Fachgruppe Biokatalyse
Einsiedlerstrasse 31a
8820 Wädenswil
Arbeit an der ZHAW
Tätigkeit
Bioinformatiker (Wissenschaftlicher Mitarbeiter)
Arbeits- und Forschungsschwerpunkte
Bioinformatik, Data Science, Modellierung, molekulardynamische Simulationen & computergestütztes Enzym Design
Lehrtätigkeit
Assosciate Fellow of the Higher Education Academy
Berufserfahrung
- CTO
candidum GmbH
10 / 2022 - 08 / 2023 - Enzym Designer
candidum GmbH
12 / 2017 - 10 / 2022
Aus- und Weiterbildung
Ausbildung
- Doctor of Philosophy
Coventry University
2021 - 2023 - Master of Science / Technische Biologie
Universität Stuttgart
10 / 2018 - 09 / 2020 - Bachelor of Science / Technische Biologie
Universität Stuttgart
10 / 2015 - 09 / 2018
Netzwerk
Mitglied in Netzwerken
- NCCR Catalysis
- ESAB - European Society of Applied Biocatalysis
- Pan-European Network on Computational Redesign of Enzymes
ORCID digital identifier
Auszeichnungen
Instant Impact Fund
ZHAW sustainable
01 / 2025
Publikationen
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Stockinger, Peter; Buller, Rebecca,
2024.
Nature’s toolbox for the hydrolysis of lactams and cyclic imides.
ACS Catalysis.
14(21), S. 16055-16073.
Verfügbar unter: https://doi.org/10.1021/acscatal.4c04474
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Patsch, David; Schwander, Thomas; Voss, Moritz; Schaub, Daniela; Hüppi, Sean; Eichenberger, Michael; Stockinger, Peter; Schelbert, Lisa; Giger, Sandro; Peccati, Francesca; Jiménez-Osés, Gonzalo; Mutný, Mojmír; Krause, Andreas; Bornscheuer, Uwe T.; Hilvert, Donald; Buller, Rebecca M.,
2024.
Enriching productive mutational paths accelerates enzyme evolution.
Nature Chemical Biology.
20(12), S. 1662-1669.
Verfügbar unter: https://doi.org/10.1038/s41589-024-01712-3
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Honda Malca, Sumire; Stockinger, Peter; Duss, Nadine; Milbredt, Daniela; Iding, Hans; Buller, Rebecca,
2024.
Excelzyme : a Swiss university-industry collaboration for accelerated biocatalyst development.
Chimia.
78(3), S. 108-117.
Verfügbar unter: https://doi.org/10.2533/chimia.2024.108
Publikationen vor Tätigkeit an der ZHAW
- The Short-chain Dehydrogenase/Reductase Engineering Database (SDRED): A classification and analysis system for a highly diverse enzyme family.
- The triple variant K170D/N174L/D239A compensates the destabilizing effect of variant K170D/N174L in β-hydroxyacid dehydrogenase (βHAD) from Arabidopsis thaliana
- Crossing the Border: From Keto‐ to Imine Reduction in Short‐Chain Dehydrogenases/Reductases
- Systematic Evaluation of Imine‐Reducing Enzymes: Common Principles in Imine Reductases, β‐Hydroxy Acid Dehydrogenases, and Short‐Chain Dehydrogenases/ Reductases
- Engineering of Thermostable β‐Hydroxyacid Dehydrogenase for the Asymmetric Reduction of Imines
- Inverting the Stereoselectivity of an NADH‐Dependent Imine‐Reductase Variant