Martin-Luther-Universität Halle-Wittenberg

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Publikationen

2016

van Herwijnen, H. W. G., Krug, D., Mäbert, M., Büttner, K., Jacob, M. und Pietzsch, M. (2016). “Renewable wood adhesives based on cross-linkable protein.” holztechnologie, 57, 12-16.

2015

Ulrich, J., and Pietzsch, M. (2015). “What is a protein crystal? Can we apply the terminology of classical industrial crystallization to them?” Cryst. Res. Technol, 50, 560–565. http://dx.doi.org/10.1002/crat.201500057   

Witting, M., Obst, K., Pietzsch, M., Friess, W. and Hedtrich, S. (2015). “Feasibility Study for Intra-Epidermal Delivery of Proteins Using A Solid Microneedle Array” International Journal of Pharmaceutics, 486, 52–58. http://dx.doi.org/10.1016/j.ijpharm.2015.03.046   

Malešević, M., Migge, A., Hertel, T. C. and Pietzsch, M. (2015). “A Fluorescence-based Array Screen for Transglutaminase Substrates.” ChemBioChem., 16, 1169 – 1174.

2014

Liu, Y., Pietzsch, M., and Ulrich, J. (2014), “Determination of the phase diagram for the crystallization of L-asparaginase II by a turbidity technique” Cryst. Res. Technol. 49, 262–268.

2013

Weichert, N., Hauptmann, V., Menzel, M., Schallau, K., Gunkel, P., Hertel, T. C., Pietzsch, M., Spohn, U. und Conrad, U. (2013). “Transglutamination allows production and characterization of native-sized ELPylated spider silk proteins from transgenic plants.” Plant Biotechnol J., 12, 265–275.

Toufik Naolou, Annette Meister, Regina Schöps, Markus Pietzsch, and Jörg Kressler (2013), „Synthesis and characterization of graft copolymers able to form polymersomes and worm-like aggregates”, Soft Matter, 9, 10364-10372.

Liu, Y., Pietzsch, M., and Ulrich, J. (2013), “Purification of L-asparaginase II by crystallization” Front. Chem. Sci. Eng., 7, 37-42.

2012

Stolte, I., Frohberg, P., Pietzsch, M., and Ulrich, J. (2012). „Crystals in protein films: What are they good for?” Chemical Engineering Science   , 77, 196-200.

Buettner, K., Hertel, T. C. und Pietzsch, M. (2012). “Increased thermostability of microbial transglutaminase by combination of several hot spots evolved by random and saturation mutagenesis.” Amino Acids, 42, 987-996.

Sommer, C., Hertel, T. C., Schmelzer, C. E. H. und Pietzsch, M. (2012). “Investigations on the activation of recombinant microbial pro-transglutaminase: In contrast to Proteinase K, Dispase removes the Histidine-tag.” Amino Acids, 42, 997-1006.

2011

Müller, C., Liu, Y., Migge, A., Pietzsch, M. and Ulrich, J. (2011). “Recombinant L-Asparaginase B and its Crystallization – What is the Nature of Protein Crystals?” J. Chem. Eng. Tech., 34, 571–577.

Sommer, C., Volk, N. and Pietzsch, M. (2011). “Model based optimization of the fed-batch production of a highly active transglutaminase variant in E. coli.” Protein Expression and Purification, 77, 9–19.

2010

Fuchs, S., Kutscher, M., Hertel, T., Winter, G., Pietzsch, M. and Coester, C. (2010). “Transglutaminase: new insights into gelatin nanoparticle cross-linking.” Journal of Microencapsulation, 27, 747-754.

Patzsch, K., Riedel, K. and Pietzsch, M. (2010). “Parameter optimization for protein film production using microbial transglutaminase.” Biomacromolecules, 11, 896 – 903.

Patzsch, K., Riedel, K. and Pietzsch, M. (2010). “Untersuchungen zur Herstellung von Folien aus nachwachsenden Rohstoffen durch enzymkatalysierte Vernetzung von Proteinen.” Chemie Ingenieur Technik, 82, 87 – 92.

Büttner, K., Marx, C., Hertel, T. and Pietzsch, M. (2010). “Optimierung einer rekombinanten mikrobiellen Transglutaminase.” Chemie Ingenieur Technik. 82, 43-49.

2009

Besheer, A., Hertel, T. C., Kressler, J., Mäder, K., and Pietzsch, M. (2009). “Enzymatically-catalyzed HESylation using microbial transglutaminase: Proof of feasibility.” Journal of Pharmaceutical Sciences 98, 4420-4428.

2008

Marx, C., Hertel, T. und Pietzsch, M. (2008). “Random mutagenesis of a recombinant microbial transglutaminase for the generation of thermostable and heat-sensitve variants”, J. Biotechnol.,   136, 156–162. http://dx.doi.org/10.1016/j.jbiotec.2008.06.005   

Marx, C., Hertel, T. und Pietzsch, M. (2008). “Purification and activation of a recombinant histidine-tagged pro-transglutaminase after soluble expression in E. coli and characterization of the active enzyme.” Enz. Microb.Technol., 42, 568-575. http://dx.doi.org/10.1016/j.enzmictec.2008.03.003   

Gerber, S., Kirchhof, K., Kressler, J., Schmelzer, C. E. H., Scholz, C., Hertel, T. und Pietzsch, M. (2008). “Cloning, expression, partial purification and characterization of a designer protein with repetitive sequences.” Journal of Protein Expression and Purification. 59, 203-214. http://dx.doi.org/10.1016/j.pep.2008.01.022.   

2007

Gerber, S., Kirchhof, K., Kressler, J., Schmelzer, C. E. H., Scholz, C., Hertel, T. C., Pietzsch, M. Preparation and characterization of an artificial peptide with repetitive sequences. Abstracts of Papers, 234th ACS National Meeting, Boston, MA, United States, August 19-23, 2007 (2007), PMSE-018.

Marx, C., Hertel, T. and Pietzsch, M. (2007). “Soluble expression of a pro-transglutaminase from Streptomyces mobaraensis in Escherichia coli.” Enz. Microb. Technol., 40, 1543 - 1550.

2005

Dette, S. S., Jones, M. J., Pietzsch, M., Hertel, T. und Ulrich, J. (2005). “Protein Activity as a Measure of Quality in the Batch Crystallization of Lysozyme.” In: Conference Proceedings 16th International Symposium on Industrial Crystallization (Ulrich, J., ed.), VDI Verlag, Düsseldorf, 861-865, Vol 16.

Jones, M. J., Pietzsch, M.; Hertel, T. Ulrich, J. (2005).
„Investigation of crystallization conditions for porcine trypsin“, In: Conference Proceedings 16th International Symposium on Industrial Crystallization, September, 11 - 14, International Congress Center, Dresden, Germany ; 2. - Dresden : VDI-Verl.. - 2005, S. 683-688.

Weber, M., Jones, M. J., Hertel, T., Pietzsch, M., Ulrich, J. (2005). „An improved protein solubility measurement method : Solubility of hen egg white lysozyme“, In: Proceedings of the 12. International Workshop on Industrial Crystallization. - Halle (Saale). – VDI-Verl. 2005, S. 232-239.

Wiemann, A., Anton, W.,
Schnabel, R. und Pietzsch, M. (2005). “New Materials by enzymatical cross-linking of proteins from renewable resources. Conference Proceedings 4th Green-Tech Conference, Landwirtschaftsverlag GmbH, Münster, Germany, in “Nachwachsende Rohstoffe”, vol. 27, 491- 493

Weber, M., Jones, M. J., Pietzsch, M., Hertel, T. und Ulrich, J. (2005).
“Purification of Urease by Crystallization.” In: Conference Proceedings 16th International Symposium on Industrial Crystallization (ISIC) Dresden (Ulrich, J., ed.), VDI Verlag, Düsseldorf, 23-28, Vol 16.

2002

Vasil´ev, A. A., Vielhauer, O., Engman, L., Pietzsch, M., Serebryakov, E. P. (2002), „Enzymatic dissymmetrization of meso-2,3-dimethylbutane-1,4-diol and its diacetate. Synthesis of scalemic (-)-lasiol. Russ. Chem. Bull. Int. Ed., 51, 481-487.

2001

Ragnitz, K., Syldatk, C. und Pietzsch, M. (2001). “Optimization of the immobilization parameters and operational stability of immobilized hydantoinase and L-N-carbamoylase from Arthrobacter aurescens for the production of optically pure L-amino acids.” Enzyme Microb. Technol. 28, 713-720.

Ragnitz, K.; Syldatk, C. and Pietzsch, M. (2001) “Immobilization of the hydantoin-cleaving enzymes from Arthrobacter aurescens DSM 3747.”, J. Biotechnol, 92, 179-186.

Smith, R. J., Pietzsch, M., Waniek, T., Syldatk, C. und Bienz, S. (2001) “Microbial and enzymatic synthesis of enantiomerically enriched D- and L-silylated alanines by deracemization of D,L-5-silylmethylated hydantoins”, Tetrahedron: Asymmetry, 12, 157-165.

2000

Beumer, R., Bubert, C., Cabrele, C., Vielhauer, O., Pietzsch, M. und Reiser, O. (2000). “The synthesis of diastereo- and enantiomerically pure ß-aminocyclopropane carboxylic acids.” J. Org. Chem., 65, 8960-8969.

Wiese, A.; Pietzsch, M.; Syldatk, C.; Mattes, R. and Altenbuchner, J. (2000). “Hydantoin-racemase from Arthrobacter aurescens DSM 3747 - Heterologous expression, purification and characterization.”, J. Biotechnol., 80, 217-230.

Pietzsch, M.; Waniek, T.; Smith, R. J.; Bratovanov, S.; Bienz, S. and Syldatk, C. (2000). “Microbial and enzymatic synthesis of optically pure D- and L-3-trimethylsilyl-alanine by deracemization of D,L-5-trimethylsilyl-hydantoin.”, Chemical Monthly, 131, 645-653.

Pietzsch, M.; Wiese, A.; Ragnitz, K.; Wilms, B.; Altenbuchner, J.; Mattes, R. and Syldatk, C. (2000). “Purification of recombinant hydantoinase and L-N-carbamoylase from Arthrobacter aurescens expressed in Escherichia coli: Comparison of wild-type and genetically modified proteins.”, J. Chromatogr. B, 737, 179-186.

1999

Pietzsch, M.; Vielhauer, O.; Pamperin, D.; Ohse, B. and Hopf, H. (1999). “On the kinetics of the enzyme-catalyzed hydrolysis of axial chiral alkylallenecarboxylates: Preparation of S-(+)-2-ethyl-4-phenyl-2,3-hexadiene carboxylic acid methylester.”, J. Molec. Catal. B: Enzymatic, 6, 51-57.

Wilms, B.; Wiese, A.; Syldatk, C.; Mattes, R.; Altenbuchner, J. and Pietzsch, M. (1999). “Cloning, nucleotide sequence and expression of a new L-N-carbamoylase gene from Arthrobacter aurescens DSM 3747 in E. coli.”, J. Biotechnol., 68, 101-113.

Teves, H.; Waniek, T.; Pietzsch, M.; Syldatk, C. and Reuss, M. (1999). “Application of different polarimetric methods for the analysis of enzyme-catalyzed enantioselective reactions.”, Fresenius J. Anal. Chem., 363, 738-743.

1998

Pamperin, D.; Schulz, C.; Hopf, H.; Syldatk, C. and Pietzsch, M. (1998b). “Chemoenzymatic synthesis of optically pure planar chiral (S)-(-)-5-formyl-4-hydroxy[2.2]paracyclophane.”, Eur. J. Org. Chem., 1441-1445.

Pamperin, D.; Ohse, B.; Hopf, H. and Pietzsch, M. (1998a). “Synthesis of planar-chiral [2.2]paracyclophanes by biotransformations: Screening for hydrolase activity for the kinetic resolution of 4-acetoxy-[2.2]paracyclophane.”, J. Molec. Catal. B: Enzymatic, 5, 317-319.

Kroutil, W.; Genzel, Y.; Pietzsch, M.; Syldatk, C. and Faber, K. (1998). “Purification, characterization and stabilization of a highly selective epoxide hydrolase from Nocardia sp. EH1.”, J. Biotechnol., 61, 143-150.

Siemann, M.; Alvarado-Marín, Á.; Pietzsch, M. and Syldatk, C. (1999). “A D-specific hydantoin amidohydrolase: Properties of the metalloenzyme purified from Arthrobacter crystallopoietes.”, J. Molec. Catal. B: Enzymatic, 6, 387-397.

May, O.; Siemann, M.; Pietzsch, M.; Kiess, M.; Mattes, R. and Syldatk, C. (1998). “Substrate-dependent enantioselectivity of a novel hydantoinase from Arthrobacter aurescens DSM 3745: Purification and characterisation as new member of cyclic amidases.”, J. Biotechnol., 61, 1-13.

1997

Pamperin, D.; Hopf, H.; Syldatk, C. and Pietzsch, M. (1997). “Synthesis of planar chiral [2.2]paracyclophanes by biotransformations: Kinetic resolution of 4-formyl-[2.2]paracyclophane by asymmetric reduction.”, Tetrahedron: Asymmetry, 8, 319-325.

1996

Cai, J.; Pietzsch, M.; Theobald, U. and Rizzi, M. (1996). “Fast purification and kinetic studies of the glycerol-3-phosphate dehydrogenase from the yeast Saccharomyces cerevisiae.”, J. Biotechnol., 49, 19-27.

Huber, P.; Bratovanov, B.; Bienz, S.; Syldatk, C. and Pietzsch, M. (1996). “Chiral silicon groups as auxiliaries for enantioselective synthesis: Access to optically active silanes by biotransformation and the enantiospecific preparation of (R)-(+)-1-Phenylethanol.”, Tetrahedron: Asymm., 7, 69-78.

Cai, J.; Pietzsch, M. and Rizzi, M. (1996). “Induced formation, purification and properties of glycerol-3-phosphate dehydrogenase from Saccharomyces cerevisiae.”, Acta Mycolog. Sinica, 15, 121-128.

1994

Bückmann, A. F.; Erdmann, H.; Pietzsch, M.; Hall, J. M. and Bannister, J. V. (1994). “N6-(2-Aminoethyl)-FAD: Synthesis and coenzyme activity with respect to APO-NADH oxidase from Thermus thermophilus and Thermus aquaticus.”, Flavins and Flavoproteins, Walter de Gruyter & Co., Berlin, 597-600.

1992

Bunge, F.; Pietzsch, M.; Müller, R. and Syldatk, C. (1992). “Mechanical disruption of Arthrobacter sp. DSM 3747 in stirred ball mills for the release of hydantoin-cleaving enzymes.”, Chem. Eng. Sci., 47, 225-232.

Pietzsch, M.; Syldatk, C. and Wagner, F. (1992). “A new racemase for 5-monosubstituted hydantoins.”, Ann. N. Y. Acad. Sci., 672, 478-483.

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