TY  - BOOK
A1  - Berg, G.
A1  - Gaul, G.
A1  - Hagedoorn, H.
A1  - Hardt, Arno
A1  - Heide, J. A. van der
A1  - Hinterberger, F.
A1  - Huber, Max
A1  - Jahn, R.
A1  - Martin, S.
A1  - Mayer-Kuckuk, T.
A1  - Osterfeld, F.
A1  - Paetz gen. Schieck, H.
A1  - Prasuhn, D.
A1  - Riepe, G.
A1  - Rogge, M.
A1  - Rossen, P. von
A1  - Schult, O. W. B.
A1  - Speth, J.
A1  - Turek, P.
T1  - Studie zum Bau eines kombinierten Kühler-Synchrotron-Rings an der KFA Jülich: COSY-Studie. Spezielle Berichte der Kernforschungsanlage Jülich. Nr. 0242. Jül-Spez-242
Y1  - 1984
PB  - Kernforschungsanlage
CY  - Jülich
ER  - 
TY  - CHAP
A1  - Martin, S.
A1  - Berg, G.
A1  - Hardt, Arno
A1  - Hürlimann, W.
A1  - Köhler, M.
A1  - Meißberger, J.
A1  - Sagefka, T.
A1  - Schult, O. W. B.
ED  - Sanderson, N. E.
T1  - First experience with the magnet spectrometer 'BIG KARL'
T2  - Use of magnetic spectrometers in nuclear physics : proceedings of the Daresbury study weekend 10 - 11 March 1979
Y1  - 1979
SP  - 38
EP  - 42
PB  - Daresbury Lab.
CY  - Daresbury
ER  - 
TY  - JOUR
A1  - Ribitsch, D.
A1  - Heumann, S.
A1  - Karl, W.
A1  - Gerlach, J.
A1  - Leber, R.
A1  - Birner-Gruenberger, R.
A1  - Gruber, K.
A1  - Eiteljoerg, I.
A1  - Remler, P.
A1  - Siegert, Petra
A1  - Lange, J.
A1  - Maurer, Karl-Heinz
A1  - Berg, G.
A1  - Guebitz, G. M.
A1  - Schwab, H.
T1  - Extracellular serine proteases from Stenotrophomonas maltophilia: Screening, isolation and heterologous expression in E. coli
JF  - Journal of biotechnology
N2  - 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.
KW  - Alginate beads
KW  - Stenotrophomonas maltophilia
KW  - Detergent protease
Y1  - 2012
U6  - http://dx.doi.org/10.1016/j.jbiotec.2011.09.025
SN  - 1873-4863 (E-Journal); 0168-1656 (Print)
VL  - 157
IS  - 1
SP  - 140
EP  - 147
PB  - Elsevier
CY  - Amsterdam
ER  -