Enzyme Immobilization on Polypropylene Film: A Role Model for Biocatalytic Polymer Membranes?
Gartner, P.; Rudat, J.; Bilger, M.; Gruenert, T.; Lanza, G.
2023. Journal of Enzymes, 1 (3), 1–12. doi:10.14302/issn.2690-4829.jen-23-4799

Development of two devices for high-throughput screening of ethanol-producing microorganisms by real-time CO₂ production monitoring
Gord Noshahri, N.; Sharifi, A.; Seyedabadi, M.; Rudat, J.; Zare Mehrjerdi, M.
2023. Bioprocess and Biosystems Engineering, 46 (8), 1209–1220. doi:10.1007/s00449-023-02892-3

Self-healing Fuel Cells by Biological Actuators
Gartner, P.; Lanza, G.; Rudat, J.; Bilger, M.; Grünert, T.; Nesterov-Mueller, A.; Zimmerer, N.; Quarz, P.; Scharfer, P.; Schabel, W.; Jung, A. P.; Stahlberger, M.; Bräse, S.
2023. Procedia CIRP, 116, 161–166. doi:10.1016/j.procir.2023.02.028

Selective Peptide Binders to the Perfluorinated Sulfonic Acid Ionomer Nafion
Schmidt, D.; Gartner, P.; Berezkin, I.; Rudat, J.; Bilger, M.; Grünert, T.; Zimmerer, N.; Quarz, P.; Scharfer, P.; Brückel, J.; Jung, A. P.; Singh, P.; Pooja, P.; Meier, B.; Stahlberger, M.; Schabel, W.; Bräse, S.; Lanza, G.; Nesterov-Mueller, A.
2023. Advanced Functional Materials, Article no: 2214932. doi:10.1002/adfm.202214932

Origin and Evolution of Enzymes with MIO Prosthetic Group: Microbial Coevolution After the Mass Extinction Event
Peng, F.; Engel, U.; Aliyu, H.; Rudat, J.
2022. Frontiers in Genetics, 13, Art.-Nr. 851738. doi:10.3389/fgene.2022.851738

Enzymatic Synthesis of Alkyl Glucosides by β‐Glucosidases in a 2‐in‐1 Deep Eutectic Solvent System 
Delavault, A.; Grüninger, J.; Kapp, D.; Hollenbach, R.; Rudat, J.; Ochsenreither, K.; Syldatk, C.
2022. Chemie - Ingenieur - Technik, 94 (3), 417–426. doi:10.1002/cite.202100150

Enhanced Bioactivity of Tailor-Made Glycolipid Enriched Manuka Honey
Delavault, A.; Zoheir, A. E.; Muller, D.; Hollenbach, R.; Rabe, K. S.; Ochsenreither, K.; Rudat, J.; Syldatk, C.
2022. International Journal of Molecular Sciences, 23 (19), Art.-Nr.: 12031. doi:10.3390/ijms231912031

Synthesis of (S)- and (R)-β-Tyrosine by Redesigned Phenylalanine Aminomutase
Peng, F.; Aliyu, H.; Delavault, A.; Engel, U.; Rudat, J.
2022. Catalysts, 12 (4), Art.-Nr.: 397. doi:10.3390/catal12040397

Biotechnologische Synthese und Transformation nicht-kanonischer Aminosäuren : neue Mikroorganismen und optimierte Enzyme - nachhaltige Substrate und effiziente (Hochdurchsatz-)Analytik - bioinformatorische Modellierung und innovative Produktionsverfahren. habilitation thesis
Rudat, J.
2021. Karlsruher Institut für Technologie (KIT)

Alanins Wunderlampe : Vorkommen, Nutzung und Produktion nicht-kanonischer Aminosäuren
Rudat, J.; Engel, U.
2021. Biologie in unserer Zeit, 51 (4), 376–386. doi:10.11576/ biuz-4827

Computational-designed enzyme for β-tyrosine production in lignin valorization
Peng, F.; Aliyu, H.; Delavault, A.; Engel, U.; Rudat, J.
2021. Catalysts, 11 (11), 1310. doi:10.3390/catal11111310

Comparative study on interfacial and foaming properties of glycolipids in relation to the gas applied for foam generation
Hollenbach, R.; Oeppling, S.; Delavault, A.; Völp, A. R.; Willenbacher, N.; Rudat, J.; Ochsenreither, K.; Syldatk, C.
2021. RSC Advances, 11 (54), 34235–34244. doi:10.1039/D1RA06190A

Growth optimization and identification of an ω-transaminase by a novel native PAGE activity staining method in a Bacillus sp. strain BaH isolated from Iranian soil
Gord Noshahri, N.; Fooladi, J.; Engel, U.; Muller, D.; Kugel, M.; Gorenflo, P.; Syldatk, C.; Rudat, J.
2021. AMB Express, 11 (1), Art.-Nr.: 46. doi:10.1186/s13568-021-01207-7

Interfacial and Foaming Properties of Tailor-Made Glycolipids—Influence of the Hydrophilic Head Group and Functional Groups in the Hydrophobic Tail
Hollenbach, R.; Völp, A. R.; Höfert, L.; Rudat, J.; Ochsenreither, K.; Willenbacher, N.; Syldatk, C.
2020. Molecules, 25 (17), 3797. doi:10.3390/molecules25173797

Screening and comparative characterization of microorganisms from Iranian soil samples showing ω-transaminase activity toward a plethora of substrates
Noshahri, N. G.; Fooladi, J.; Syldatk, C.; Engel, U.; Heravi, M. M.; Mehrjerdi, M. Z.; Rudat, J.
2019. Catalysts, 9 (10), Article No.874. doi:10.3390/catal9100874

Improvement in the Thermostability of a β-Amino Acid Converting ω-Transaminase by Using FoldX
Buß, O.; Muller, D.; Jager, S.; Rudat, J.; Rabe, K. S.
2018. ChemBioChem, 19 (4), 379–387. doi:10.1002/cbic.201700467

Enantiomer discrimination in β-phenylalanine degradation by a newly isolated Paraburkholderia strain BS115 and type strain PsJN
Buß, O.; Dold, S.-M.; Obermeier, P.; Litty, D.; Muller, D.; Grüninger, J.; Rudat, J.
2018. AMB express, 8 (1), Article: 149. doi:10.1186/s13568-018-0676-2

β-Phenylalanine Ester Synthesis from Stable β-Keto Ester Substrate Using Engineered ω-Transaminases
Buß, O.; Voss, M.; Delavault, A.; Gorenflo, P.; Syldatk, C.; Bornscheuer, U.; Rudat, J.
2018. Molecules, 23 (5), Article: 1211. doi:10.3390/molecules23051211

The ω-transaminase engineering database (oTAED) : A navigation tool in protein sequence and structure space
Buß, O.; Buchholz, P. C. F.; Gräff, M.; Klausmann, P.; Rudat, J.; Pleiss, J.
2018. Proteins, 86 (5), 566–580. doi:10.1002/prot.25477

FoldX as Protein Engineering Tool: Better Than Random Based Approaches?
Buß, O.; Rudat, J.; Ochsenreither, K.
2018. Computational and structural biotechnology journal, 16, 25–33. doi:10.1016/j.csbj.2018.01.002

Toward a cell-free hydantoinase process : screening for expression optimization and one-step purification as well as immobilization of hydantoinase and carbamoylase
Slomka, C.; Späth, G. P.; Lemke, P.; Skoupi, M.; Niemeyer, C. M.; Syldatk, C.; Rudat, J.
2017. AMB express, 7 (1), Art. Nr. 122. doi:10.1186/s13568-017-0420-3

Phenylalanine ammonia lyase from Arabidopsis thaliana (AtPAL2) : A potent MIO-enzyme for the synthesis of non-canonical aromatic alpha-amino acids. Part I: Comparative characterization to the enzymes from Petroselinum crispum (PcPAL1) and Rhodosporidium toruloides (RtPAL)
Dreßen, A.; Hilberath, T.; Mackfeld, U.; Billmeier, A.; Rudat, J.; Pohl, M.
2017. Journal of biotechnology, 258, 148–157. doi:10.1016/j.jbiotec.2017.04.005

Phenylalanine ammonia lyase from Arabidopsis thaliana (AtPAL2) : A potent MIO-enzyme for the synthesis of non-canonical aromatic alpha-amino acids.. Part II: Application in different reactor concepts for the production of (S)-2-chloro-phenylalanine
Dreßen, A.; Hilberath, T.; Mackfeld, U.; Rudat, J.; Pohl, M.
2017. Journal of biotechnology, 258, 158–166. doi:10.1016/j.jbiotec.2017.04.035

Hydantoinasen – von der präbiotischen Evolution zur Aminosäureproduktion
Rudat, J.; Engel, U.
2017. Biospektrum, 23 (1), 98–100. doi:10.1007/s12268-017-0770-z

Transaminases and their applications
Dold, S.-M.; Syldatk, C.; Rudat, J.
2016. Green biocatalysis. Ed.: R. Patel, 715–746, Wiley-VCH Verlag. doi:10.1002/9781118828083.ch29

One-step purification and immobilization of a β-amino acid aminotransferase using magnetic (M-PVA) beads
Dold, S.-M.; Cai, L.; Rudat, J.
2016. Engineering in life sciences / Special Issue: Molecular Interaction Engineering, 16 (6), 568–576. doi:10.1002/elsc.201600042

Stereoselective synthesis of β-amino acids by hydrolysis of an aryl-substituted dihydropyrimidine by hydantoinases
Engel, U.; Syldatk, C.; Rudat, J.
2016. Practical Methods for Biocatalysis and Biotransformations 3. Ed.: J. Whittall, John Wiley and Sons

Statistical Evaluation of HTS Assays for Enzymatic Hydrolysis of β-Keto Esters
Buß, O.; Jager, S.; Dold, S. M.; Zimmermann, S.; Hamacher, K.; Schmitz, K.; Rudat, J.
2016. PLoS one, 11 (1), e0146104. doi:10.1371/journal.pone.0146104

Chemical synthesis and enzymatic, stereoselective hydrolysis of a functionalized dihydropyrimidine for the synthesis of β-amino acids
Slomka, C.; Zhong, S.; Fellinger, A.; Engel, U.; Syldatk, C.; Bräse, S.; Rudat, J.
2015. AMB Express, 5 (1), 85. doi:10.1186/s13568-015-0174-8

Hydrolysis of Hydantoins, Dihydropyrimidines, and Related Compounds
Slomka, C.; Engel, U.; Syldatk, C.; Rudat, J.
2015. Biocatalysis in Organic Synthesis 1. Ed.: K. Faber, 373–414, Thieme Gruppe

The Hydantoinase Process: Recent developments for the production of non-canonical amino acids
Engel, U.; Rudat, J.; Syldatk, C.
2014. Industrial biocatalysis. Ed.: P. Grunwald, Chapter 22, 817–862, Pan Stanford Publ

Cationic heterooligopeptides by ficain-catalyzed co-oligomerization of lysine and methionine ethylesters
Andre, M.; Kühl, B.; Brenner-Weiss, G.; Syldatk, C.; Rudat, J.
2014. Journal of peptide science, 20, 625–629. doi:10.1002/psc.2639

Enzymatical and microbial degradation of cyclic dipeptides (diketopiperazines)
Perzborn, M.; Syldatk, C.; Rudat, J.
2013. AMB Express, 3 (1), 12 S. doi:10.1186/2191-0855-3-51

Separation of Cyclic Dipeptides (Diketopiperazines) from Their Corresponding Linear Dipeptides by RP-HPLC and Method Validation
Perzborn, M.; Syldatk, C.; Rudat, J.
2013. Chromatography research international, 2013, 310269. doi:10.1155/2013/310269

Transaminases for the synthesis of enantiopure beta-amino acids
Rudat, J.; Brucher, B.; Syldatk, C.
2012. AMB Express, 2 (1), 11. doi:10.1186/2191-0855-2-11

Stereoselective hydrolysis of aryl-substituted dihydropyrimidines by hydantoinases
Engel, U.; Syldatk, C.; Rudat, J.
2012. Applied microbiology and biotechnology, 94 (5), 1221–1231. doi:10.1007/s00253-011-3691-7

Novel amidases of two Aminobacter sp. strains: Biotransformation experiments and elucidation of gene sequences
Engel, U.; Syldatk, C.; Rudat, J.
2012. AMB express, 2 (1), 33. doi:10.1186/2191-0855-2-33

Food safety: Heat inactivation of Cronobacter in powdered infant formula
Baumann, S.; Rudat, J.
2011. International Journal of Medical Microbiology, 301, 59/1–1

Synthesis of aromatic beta-amino-acid with new cyclic amidases
Bretschneider, U.; Syldatk, C.; Rudat, J.
2010. Chemie Ingenieur Technik, 82 (1-2), 161–165

Microbial conversion of B-Phenyl-alanine using new transaminase
Brucher, B.; Syldatk, C.; Rudat, J.
2010. Chemie Ingenieur Technik, 82, 155–160

Enantioseparation of Aromatic beta(A3)-Amino acid by Precolumn Derivatization with o-Phthaldialdehyde and N-Isobutyryl-l-cysteine
Brucher, B.; Rudat, J.; Syldatk, C.; Vielhauer, O.
2010. Chromatographia, 71 (11-12), 1063–1067. doi:10.1365/s10337-010-1578-x