@misc{RothTippkoetter2016,
  author    = {Roth, J. and Tippk{\"o}tter, Nils},
  title     = {New Approach for Enzymatic Hydrolysis of Lignocellulose with Selective Diffusion Separation of the Monosaccharide Products},
  series = {Chemie Ingenieur Technik},
  volume    = {88},
  journal   = {Chemie Ingenieur Technik},
  number    = {9},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {0009-286X},
  doi       = {10.1002/cite.201650301},
  pages     = {1237},
  year      = {2016},
  abstract  = {Enzymatic hydrolysis of lignocellulosic material plays an important role in the classical biorefinery approach. Apart from the pretreatment of the raw material, hydrolysis is the basis for the conversion of the cellulose and hemicellulose fraction into fermentable sugars. After hydrolysis, usually a solid-liquid separation takes place, in order to separate the residual plant material from the sugar-rich fraction, which can be subsequently used in a fermentation step. In order to factor out the separation step, the usage of in alginate immobilized crude cellulose fiber beads (CFBs) were evaluated. Pretreated cellulose fibers are incorporated in an alginate matrix together with the relevant enzymes. In doing so, sugars diffuse trough the alginate matrix, allowing a simplified delivery into the surrounding fluid. This again reduces product inhibition of the glucose on the enzyme catalysts. By means of standardized bead production the hydrolysis in lab scale was possible. First results show that liberation of glucose and xylose is possible, allowing a maximum total sugar yield of 75 \%.},
  language  = {en}
}
@article{OehlenschlaegerVolkmarStiefelmaieretal.2024,
  author    = {Oehlenschl{\"a}ger, Katharina and Volkmar, Marianne and Stiefelmaier, Judith and Langsdorf, Alexander and Holtmann, Dirk and Tippk{\"o}tter, Nils and Ulber, Roland},
  title     = {New insights into the influence of pre-culture on robust solvent production of C. acetobutylicum},
  series = {Applied Microbiology and Biotechnology},
  volume    = {108},
  journal   = {Applied Microbiology and Biotechnology},
  publisher = {Springer},
  address   = {Berlin, Heidelberg},
  issn      = {1432-0614},
  doi       = {10.1007/s00253-023-12981-8},
  pages     = {10 Seiten},
  year      = {2024},
  abstract  = {Clostridia are known for their solvent production, especially the production of butanol. Concerning the projected depletion of fossil fuels, this is of great interest. The cultivation of clostridia is known to be challenging, and it is difficult to achieve reproducible results and robust processes. However, existing publications usually concentrate on the cultivation conditions of the main culture. In this paper, the influence of cryo-conservation and pre-culture on growth and solvent production in the resulting main cultivation are examined. A protocol was developed that leads to reproducible cultivations of Clostridium acetobutylicum. Detailed investigation of the cell conservation in cryo-cultures ensured reliable cell growth in the pre-culture. Moreover, a reason for the acid crash in the main culture was found, based on the cultivation conditions of the pre-culture. The critical parameter to avoid the acid crash and accomplish the shift to the solventogenesis of clostridia is the metabolic phase in which the cells of the pre-culture were at the time of inoculation of the main culture; this depends on the cultivation time of the pre-culture. Using cells from the exponential growth phase to inoculate the main culture leads to an acid crash. To achieve the solventogenic phase with butanol production, the inoculum should consist of older cells which are in the stationary growth phase. Considering these parameters, which affect the entire cultivation process, reproducible results and reliable solvent production are ensured.},
  language  = {en}
}
@inproceedings{KalbeKuropkaMeyerStorketal.1988,
  author    = {Kalbe, Jochen and Kuropka, Rolf and Meyer-Stork, L. Sebastian and Lauter, S. L. and H{\"o}cker, Hartwig and Berndt, Heinz},
  title     = {Identification of fine animal hair via DNA analysis},
  series = {Proceedings of the 1st International Symposium on Specialty Animal Fibers : Aachen, October 26 - 27, 1987 ; [scientific, technological and economical aspects] . - (Schriftenreihe des Deutschen Wollforschungsinstitutes an der Technischen Hochschule Aachen e.V. ; 103)},
  booktitle = {Proceedings of the 1st International Symposium on Specialty Animal Fibers : Aachen, October 26 - 27, 1987 ; [scientific, technological and economical aspects] . - (Schriftenreihe des Deutschen Wollforschungsinstitutes an der Technischen Hochschule Aachen e.V. ; 103)},
  editor    = {K{\"o}rner, Andrea},
  publisher = {Dt. Wollforschungsinst.},
  address   = {Aachen},
  issn      = {0930-3723},
  pages     = {221 -- 227},
  year      = {1988},
  language  = {en}
}
@article{KruegerGroetzingerBerndt1987,
  author    = {Kr{\"u}ger, G{\"o}tz and Gr{\"o}tzinger, Joachim and Berndt, Heinz},
  title     = {Enantiomeric resolution of amino acid derivatives on chiral stationary phases by high-performance liquid chromatography},
  series = {Journal of Chromatography A},
  volume    = {1987},
  journal   = {Journal of Chromatography A},
  number    = {397},
  issn      = {0021-9673},
  doi       = {10.1016/S0021-9673(01)85005-6},
  pages     = {223 -- 232},
  year      = {1987},
  language  = {en}
}
@article{NokiharaBerndt1978,
  author    = {Nokihara, Kiyoshi and Berndt, Heinz},
  title     = {Synthesis of hapten-polypeptide conjugates as antigen models for the N-terminal region of the α-2-chain of rabbit skin collagen},
  series = {Journal of the Royal Society of Chemistry: Perkin Transactions 1},
  volume    = {1978},
  journal   = {Journal of the Royal Society of Chemistry: Perkin Transactions 1},
  number    = {3},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1364-5463},
  doi       = {10.1039/P19780000260},
  pages     = {260 -- 263},
  year      = {1978},
  abstract  = {Synthesis of derivatives of the peptide sequence L-pyroglutamyl-L-phenylalanyl-L-aspartyl-glycyl-L-lysyl-glycyl-glycyl-glycine as the antigenic determinant representing the N-terminal non-helical region of the α-2-chain of rabbit skin collagen, and conjugation to two different polypeptide carriers, are described.},
  language  = {en}
}
@inproceedings{KroggelBerndt1984,
  author    = {Kroggel, Matthias and Berndt, Heinz},
  title     = {The 0-hydroxiphenyloxicarbonyl-group a new base labile amine protecting group},
  series = {Peptides 1984 : Proceedings of the 18th European Peptide Symposium Djur{\"o}n{\"a}set, Sweden, June 10 - 15, 1984},
  booktitle = {Peptides 1984 : Proceedings of the 18th European Peptide Symposium Djur{\"o}n{\"a}set, Sweden, June 10 - 15, 1984},
  editor    = {Ragnarsson, Ulf},
  publisher = {Almquist \& Wiksell},
  address   = {Stockholm},
  isbn      = {91-22-00715-6},
  pages     = {81 -- 83},
  year      = {1984},
  language  = {en}
}
@article{ScheerKapelyukhRodeetal.2012,
  author    = {Scheer, Nico and Kapelyukh, Yury and Rode, Anja and Buechel, Sandra and Wolf, C. Roland},
  title     = {Generation and characterization of novel cytochrome P450 Cyp2c gene cluster knockout and CYP2C9 humanized mouse lines},
  series = {Molecular Pharmacology},
  volume    = {82},
  journal   = {Molecular Pharmacology},
  number    = {6},
  publisher = {ASPET},
  address   = {Bethesda, Md.},
  issn      = {1521-0111},
  doi       = {10.1124/mol.112.080036},
  pages     = {1022 -- 1029},
  year      = {2012},
  abstract  = {Compared with rodents and many other animal species, the human cytochrome P450 (P450) Cyp2c gene cluster varies significantly in the multiplicity of functional genes and in the substrate specificity of its enzymes. As a consequence, the use of wild-type animal models to predict the role of human CYP2C enzymes in drug metabolism and drug-drug interactions is limited. Within the human CYP2C cluster CYP2C9 is of particular importance, because it is one of the most abundant P450 enzymes in human liver, and it is involved in the metabolism of a wide variety of important drugs and environmental chemicals. To investigate the in vivo functions of cytochrome P450 Cyp2c genes and to establish a model for studying the functions of CYP2C9 in vivo, we have generated a mouse model with a deletion of the murine Cyp2c gene cluster and a corresponding humanized model expressing CYP2C9 specifically in the liver. Despite the high number of functional genes in the mouse Cyp2c cluster and the reported roles of some of these proteins in different biological processes, mice deleted for Cyp2c genes were viable and fertile but showed certain phenotypic alterations in the liver. The expression of CYP2C9 in the liver also resulted in viable animals active in the metabolism and disposition of a number of CYP2C9 substrates. These mouse lines provide a powerful tool for studying the role of Cyp2c genes and of CYP2C9 in particular in drug disposition and as a factor in drug-drug interaction.},
  language  = {en}
}
@article{BerndtKrueger1985,
  author    = {Berndt, Heinz and Kr{\"u}ger, G{\"o}tz},
  title     = {Resolution of enantiomeric amino acid derivatives by high-performance liquid chromatography on chiral stationary phases},
  series = {Journal of chromatography A},
  volume    = {1985},
  journal   = {Journal of chromatography A},
  number    = {348},
  issn      = {0021-9673},
  doi       = {10.1016/S0021-9673(01)92461-6},
  pages     = {275 -- 279},
  year      = {1985},
  language  = {en}
}
@article{KuropkaMuellerHoeckeretal.1989,
  author    = {Kuropka, Rolf and M{\"u}ller, Bettina and H{\"o}cker, Hartwig and Berndt, Heinz},
  title     = {Chiral stationary phases via hydrosilylation reaction of N-acryloylamino acids : I. Stationary phase with one chiral centre for high-performance liquid chromatography and development of a new derivatization pattern for amino acid enantiomers},
  series = {Journal of chromatography A},
  journal   = {Journal of chromatography A},
  number    = {481},
  isbn      = {0021-9673},
  pages     = {380 -- 386},
  year      = {1989},
  language  = {en}
}
@article{NokiharaBerndt1978,
  author    = {Nokihara, Kiyoshi and Berndt, Heinz},
  title     = {Studies on sulfur-containing peptides : tert-butyloxycarbonylsulfenyl and benzyloxycarbonylsulfenyl derivatives as protecting groups for cysteine},
  series = {The journal of organic chemistry},
  volume    = {43},
  journal   = {The journal of organic chemistry},
  number    = {25},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {0022-3263},
  doi       = {10.1021/jo00419a046},
  pages     = {4893 -- 4895},
  year      = {1978},
  language  = {en}
}
@article{KalbeHoeckerBerndt1989,
  author    = {Kalbe, Jochen and H{\"o}cker, Hartwig and Berndt, Heinz},
  title     = {Design of enzyme reactors as chromatographic columns for racemic resolution of amino acid esters},
  series = {Chromatographia},
  volume    = {28},
  journal   = {Chromatographia},
  number    = {3-4},
  isbn      = {0009-5893},
  doi       = {10.1007/BF02319646},
  pages     = {193 -- 196},
  year      = {1989},
  language  = {en}
}
@article{DanhoNaithaniSasakietal.1980,
  author    = {Danho, Waleed and Naithani, Vinod K. and Sasaki, Andr{\´e} N. and F{\"o}hles, Joseph and Berndt, Heinz and B{\"u}llesbach, Erika E. and Zahn, H.},
  title     = {Human proinsulin, VII : synthesis of two protected peptides corresponding to the sequences 1—45 and 46—86 of the prohormone},
  series = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {361},
  journal   = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  number    = {1},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1980.361.1.857},
  pages     = {857 -- 863},
  year      = {1980},
  language  = {en}
}
@article{KalbeKuropkaMeyerStorketal.1988,
  author    = {Kalbe, Jochen and Kuropka, Rolf and Meyer-Stork, L. Sebastian and Berndt, Heinz and Sauter, Sybille L. and Loss, Peter and Hendo, Karsten and Riesner, Detlev and H{\"o}cker, Hartwig},
  title     = {Isolation and characterization of high-molecular mass DNA from hair shafts},
  series = {Biological chemistry},
  volume    = {369},
  journal   = {Biological chemistry},
  number    = {1},
  isbn      = {0177-3593},
  doi       = {10.1515/bchm3.1988.369.1.413},
  pages     = {413 -- 416},
  year      = {1988},
  language  = {en}
}
@article{BaumannTillmannAletsee1989,
  author    = {Baumann, Marcus and Tillmann, Urban and Aletsee, Ludwig},
  title     = {Distribution of Carbon Among Photosynthetic End Products in the Bloom-Forming Arctic Diatom Thalassiosira antarctica COMBER / Tillmann, U. ; Baumann, M.E.M. ; Aletsee, L.},
  series = {Polar Biology. 10 (1989), H. 3},
  journal   = {Polar Biology. 10 (1989), H. 3},
  isbn      = {0722-4060},
  pages     = {231 -- 238},
  year      = {1989},
  language  = {en}
}
@inproceedings{AlKaidyUlberTippkoetter2014,
  author    = {Al-Kaidy, Huschyar and Ulber, Roland and Tippk{\"o}tter, Nils},
  title     = {A platform technology for the automated reaction control in magnetizable micro-fluidic droplets},
  series = {Biomaterials - made in bioreactors : book of abstracts, May 26 - 28, 2014, Radisson Blu Park Hotel and Conference Dentre, Radebeul, Germany},
  booktitle = {Biomaterials - made in bioreactors : book of abstracts, May 26 - 28, 2014, Radisson Blu Park Hotel and Conference Dentre, Radebeul, Germany},
  publisher = {DECHEMA},
  address   = {Frankfurt am Main},
  pages     = {21 -- 22},
  year      = {2014},
  language  = {en}
}
@article{HafidiElHatkaSchmitzetal.2024,
  author    = {Hafidi, Youssef and El Hatka, Hicham and Schmitz, Dominik and Krauss, Manuel and Pettrak, J{\"u}rgen and Biel, Markus and Ittobane, Najim},
  title     = {Sustainable soil additives for water and micronutrient supply: swelling and chelating properties of polyaspartic acid hydrogels utilizing newly developed crosslinkers},
  series = {Gels},
  volume    = {10},
  journal   = {Gels},
  number    = {3},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {2310-2861},
  doi       = {10.3390/gels10030170},
  pages     = {Artikel 170},
  year      = {2024},
  abstract  = {Drought and water shortage are serious problems in many arid and semi-arid regions. This problem is getting worse and even continues in temperate climatic regions due to climate change. To address this problem, the use of biodegradable hydrogels is increasingly important for the application as water-retaining additives in soil. Furthermore, efficient (micro-)nutrient supply can be provided by the use of tailored hydrogels. Biodegradable polyaspartic acid (PASP) hydrogels with different available (1,6-hexamethylene diamine (HMD) and L-lysine (LYS)) and newly developed crosslinkers based on diesters of glycine (GLY) and (di-)ethylene glycol (DEG and EG, respectively) were synthesized and characterized using Fourier transform infrared (FTIR) spectroscopy and scanning electron microscopy (SEM) and regarding their swelling properties (kinetic, absorbency under load (AUL)) as well as biodegradability of PASP hydrogel. Copper (II) and zinc (II), respectively, were loaded as micronutrients in two different approaches: in situ with crosslinking and subsequent loading of prepared hydrogels. The results showed successful syntheses of di-glycine-ester-based crosslinkers. Hydrogels with good water-absorbing properties were formed. Moreover, the developed crosslinking agents in combination with the specific reaction conditions resulted in higher water absorbency with increased crosslinker content used in synthesis (10\% vs. 20\%). The prepared hydrogels are candidates for water-storing soil additives due to the biodegradability of PASP, which is shown in an exemple. The incorporation of Cu(II) and Zn(II) ions can provide these micronutrients for plant growth.},
  language  = {en}
}
@article{RieplPettrakFaulstichetal.2010,
  author    = {Riepl, Herbert Matthias and Pettrak, J{\"u}rgen and Faulstich, Martin and Herrmann, Wolfgang Anton},
  title     = {Self metathesis of fatty alcohols and amines to provide monomers for polyester and polyamide products},
  series = {Macromolecular Symposia},
  volume    = {293},
  journal   = {Macromolecular Symposia},
  number    = {1},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1521-3900 (eISSN)},
  doi       = {10.1002/masy.200900041},
  pages     = {39 -- 42},
  year      = {2010},
  abstract  = {Self metathesis of oleochemicals offers a variety of bifunctional compounds, that can be used as monomer for polymer production. Many precursors are in huge scales available, like oleic acid ester (biodiesel), oleyl alcohol (tensides), oleyl amines (tensides, lubricants). We show several ways to produce and separate and purify C18-α,ω-bifunctional compounds, using Grubbs 2nd Generation catalysts, starting from technical grade educts.},
  language  = {en}
}
@article{HoehrPaulssenBenardetal.2014,
  author    = {Hoehr, Cornelia and Paulßen, Elisabeth and Benard, Francois and Lee, Chris Jaeil and Hou, Xinchi and Badesso, Brian and Ferguson, Simon and Miao, Qing and Yang, Hua and Buckley, Ken and Hanemaayer, Victoire and Zeisler, Stefan and Ruth, Thomas J. and Celler, Anna and Schaffer, Paul},
  title     = {⁴⁴ᶢSc production using a water target on a 13 MeV cyclotron},
  series = {Nuclear medicine and biology},
  volume    = {41},
  journal   = {Nuclear medicine and biology},
  number    = {5},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1872-9614},
  doi       = {10.1016/j.nucmedbio.2013.12.016},
  pages     = {401 -- 406},
  year      = {2014},
  abstract  = {Access to promising radiometals as isotopes for novel molecular imaging agents requires that they are routinely available and inexpensive to obtain. Proximity to a cyclotron center outfitted with solid target hardware, or to an isotope generator for the metal of interest is necessary, both of which can introduce significant hurdles in development of less common isotopes. Herein, we describe the production of ⁴⁴Sc (t₁⸝₂ = 3.97 h, Eavg,β⁺ = 1.47 MeV, branching ratio = 94.27\%) in a solution target and an automated loading system which allows a quick turn-around between different radiometallic isotopes and therefore greatly improves their availability for tracer development. Experimental yields are compared to theoretical calculations.},
  language  = {en}
}
@article{AggarwalDhimanKumaretal.2012,
  author    = {Aggarwal, Pranav and Dhiman, Shashi K. and Kumar, G. and Scherer, Ulrich W. and Singla, M. L. and Srivastava, Alok},
  title     = {Optical study of poly(ethyleneterephthalate) modified by different ionizing radiation dose},
  series = {Indian Journal of Pure and Applied Physics},
  volume    = {50},
  journal   = {Indian Journal of Pure and Applied Physics},
  number    = {2},
  publisher = {Council Of Scientific And Industrial Research (CSIR), National Institute Of Science Communication and Policy Research (NIScPR)},
  address   = {New Delhi},
  issn      = {0019-5596},
  pages     = {129 -- 132},
  year      = {2012},
  abstract  = {Thin films of poly(ethyleneterephthalate) [PET]were exposed to radiation dose ranging from 10 to 30 kGy by using gamma rays in the range 12.8-177.8 MGy using swift light ions of hydrogen. There was no effect of the radiation dose on the optical behaviour of PET as a result of exposure to radiation dose up to 30 kGy brought about by gamma rays but a significant decrease in the optical band gap values was observed when PET was exposed to swift light ions of hydrogen. The data obtained are discussed in terms of optical studies carried out on PET using swift heavy ions.},
  language  = {en}
}
@article{RibitschKarlBirnerGruenbergeretal.2010,
  author    = {Ribitsch, D. and Karl, W. and Birner-Gruenberger, R. and Gruber, K. and Eiteljoerg, I. and Remler, P. and Wieland, S. and Siegert, Petra and Maurer, Karl-Heinz and Schwab, H.},
  title     = {C-terminal truncation of a metagenome-derived detergent protease for effective expression in E. coli},
  series = {Journal of biotechnology},
  volume    = {150},
  journal   = {Journal of biotechnology},
  number    = {3},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  doi       = {10.1016/j.jbiotec.2010.09.947},
  pages     = {408 -- 416},
  year      = {2010},
  abstract  = {Recently, a new alkaline protease named HP70 showing highest homology to extracellular serine proteases of Stenotrophomonas maltophilia and Xanthomonas campestris was found in the course of a metagenome screening for detergent proteases (Niehaus et al., submitted for publication). Attempts to efficiently express the enzyme in common expression hosts had failed. This study reports on the realization of overexpression in Escherichia coli after structural modification of HP70. Modelling of HP70 resulted in a two-domain structure, comprising the catalytic domain and a C-terminal domain which includes about 100 amino acids. On the basis of the modelled structure the enzyme was truncated by deletion of most of the C-terminal domain yielding HP70-C477. This structural modification allowed effective expression of active enzyme using E. coli BL21-Gold as the host. Specific activity of HP70-C477 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 30 ± 5 U/mg compared to 8 ± 1 U/mg of the native enzyme. HP70-C477 was most active at 40 °C and pH 7-11; these conditions are prerequisite for a potential application as detergent enzyme. Determination of kinetic parameters at 40 °C and pH = 9.5 resulted in KM = 0.23 ± 0.01 mM and kcat = 167.5 ± 3.6 s⁻¹. MS-analysis of peptide fragments obtained from incubation of HP70 and HP70-C477 with insulin B indicated that the C-terminal domain influences the cleavage preferences of the enzyme. Washing experiments confirmed the high potential of HP70-C477 as detergent protease.},
  language  = {en}
}
@article{BarbazanHagenbachPaulssenetal.2010,
  author    = {Barbaz{\´a}n, Paula and Hagenbach, Adelheid and Paulßen, Elisabeth and Abram, Ulrich and Carballo, Rosa and Rodriguez-Hermida, Sabina and V{\´a}zquez-L{\´o}pez, Ezequiel M.},
  title     = {Tricarbonyl Rhenium(I) and Technetium(I) Complexes with Hydrazones Derived from 4,5-Diazafluoren-9-one and 1,10-Phenanthroline-5,6-dione},
  series = {European Journal of Inorganic Chemistry},
  journal   = {European Journal of Inorganic Chemistry},
  number    = {29},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1099-0682},
  doi       = {10.1002/ejic.201000522},
  pages     = {4622 -- 4630},
  year      = {2010},
  abstract  = {Tricarbonylrhenium(I) and -technetium(I) halide (halide = Cl and Br) complexes of ligands derived from 4,5-diazafluoren-9-one (df) and 1,10-phenanthroline-5,6-dione (phen) derivatives of benzoic and 2-hydroxybenzoic acid hydrazides have been prepared. The complexes have been characterized by elemental analysis, MS, IR, 1H NMR and absorption and emission UV/Vis spectroscopic methods. The metal centres (ReI and TcI) are coordinated through the nitrogen imine atoms and establish five-membered chelate rings, whereas the hydrazone groups stand uncoordinated. The 1H NMR spectra suggest the same behaviour in solution on the basis of only marginal variations in the chemical shifts of the hydrazine protons.},
  language  = {en}
}
@article{RibitschHeumannKarletal.2012,
  author    = {Ribitsch, D. and Heumann, S. and Karl, W. and Gerlach, J. and Leber, R. and Birner-Gruenberger, R. and Gruber, K. and Eiteljoerg, I. and Remler, P. and Siegert, Petra and Lange, J. and Maurer, Karl-Heinz and Berg, G. and Guebitz, G. M. and Schwab, H.},
  title     = {Extracellular serine proteases from Stenotrophomonas maltophilia: Screening, isolation and heterologous expression in E. coli},
  series = {Journal of biotechnology},
  volume    = {157},
  journal   = {Journal of biotechnology},
  number    = {1},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1873-4863 (E-Journal); 0168-1656 (Print)},
  doi       = {10.1016/j.jbiotec.2011.09.025},
  pages     = {140 -- 147},
  year      = {2012},
  abstract  = {A large strain collection comprising antagonistic bacteria was screened for novel detergent proteases. Several strains displayed protease activity on agar plates containing skim milk but were inactive in liquid media. Encapsulation of cells in alginate beads induced protease production. Stenotrophomonas maltophilia emerged as best performer under washing conditions. For identification of wash-active proteases, four extracellular serine proteases called StmPr1, StmPr2, StmPr3 and StmPr4 were cloned. StmPr2 and StmPr4 were sufficiently overexpressed in E. coli. Expression of StmPr1 and StmPr3 resulted in unprocessed, insoluble protein. Truncation of most of the C-terminal domain which has been identified by enzyme modeling succeeded in expression of soluble, active StmPr1 but failed in case of StmPr3. From laundry application tests StmPr2 turned out to be a highly wash-active protease at 45 °C. Specific activity of StmPr2 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 17 ± 2 U/mg. In addition we determined the kinetic parameters and cleavage preferences of protease StmPr2.},
  language  = {en}
}