TY  - JOUR
A1  - Förster, Arnold
A1  - Indlekofer, K.
A1  - Lange, J.
T1  - Theory of single-electron tunneling in resonant-tunneling diodes including scattering and multiple subbands at finite temperature / K. M. Indlekofer ; J. Lange ; A. Förster ...
JF  - Physical review / B, Condensed matter and materials physics. 53 (1996), H. 11
Y1  - 1996
SN  - 1095-3795
SP  - 7392
EP  - 7402
ER  - 
TY  - JOUR
A1  - Förster, Arnold
A1  - Lange, J.
A1  - Gerthsen, D.
T1  - The effect of growth temperature on AlAs/GaAs resonant tunnelling diodes
JF  - Journal of Physics D: Applied Physics. 27 (1994), H. 1
Y1  - 1994
SN  - 0022-3727
N1  - ISSN der E-Ausg.: 1361-6463
SP  - 175
EP  - 178
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  - 
TY  - JOUR
A1  - Förster, Arnold
A1  - Lange, J.
A1  - Gerthsen, D.
T1  - Effect of interface roughness and scattering on the performance of AlAs/InGaAs resonant tunneling diodes
JF  - Journal of Vacuum Science & Technology B: Microelectronics and Nanometer Structures. 11 (1993), H. 4
Y1  - 1993
SN  - 1071-1023
N1  - ISSN der E-Ausg.: 0734-211X
SP  - 1743
EP  - 1747
ER  -