Zobrazeno 1 - 10
of 101
pro vyhledávání: '"Volker Kasche"'
Publikováno v:
FEBS Letters. 579:5069-5073
Several factors at transcriptional, post-transcriptional or post-translational level determine the fate of a target protein and can severely restrict its yield. Here, we focus on the post-transcriptional regulation of the biosynthesis of the periplas
Publikováno v:
European Journal of Biochemistry. 270:4721-4728
Penicillin amidase from Alcaligenes faecalis is a recently identified N-terminal nucleophile hydrolase, which possesses the highest specificity constant (kcat/Km) for the hydrolysis of benzylpenicillin compared with penicillin amidases from other sou
Autor:
Volker Kasche, Boris Galunsky
Publikováno v:
Advanced Synthesis & Catalysis. 344:1115-1119
Autor:
Volker Kasche, Antje C. Spiess
Publikováno v:
Biotechnology Progress. 17:294-303
Confocal laser scanning microscopy was applied to measure the pH value in the carrier of immobilized enzymes during the enzyme-catalyzed synthesis. pH profiles with a high resolution are shown, with the pH increasing in the core of the particles. Sig
Publikováno v:
Monatshefte fuer Chemie/Chemical Monthly. 131:623-632
Publikováno v:
Enzyme and Microbial Technology. 26:165-170
Intracellular proteolysis is an important mechanism for regulating the level of the periplasmic enzyme penicillin amidase in Escherichia coli. Evidence is presented that the active enzyme is localized in the periplasmic space and maturation of pro-en
Publikováno v:
Biotechnology Letters. 22:1815-1821
The activity of immobilised soybean lipoxygenase-1 (LOX-1) was studied in aqueous and supercritical carbon dioxide (SCCO2) media for the production of 13S-hydroperoxyoctadecadenoic acid (13S-HPODE). In SCCO2, it was optimal at 33 °C and 25 MPa. A hi
Publikováno v:
Biotechnology Letters. 22:1727-1732
The yield of periplasmic enzyme, penicillin amidase (PA), from E. coli ATCC 11105 is regulated at the post-translational level by two competitive processes-intracellular proteolysis of newly synthesised pre-pro-PA (ppPA) in the cytoplasm and membrane
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1433:327-334
The pH dependence of E (enantiomeric ratio or enantioselectivity, a quantitative measure for enzyme stereospecificity) was studied for penicillin amidase catalysed hydrolysis of charged enantiomeric substrates. Theoretical analysis shows that a pH de
Autor:
Volker Kasche, Wilhelm Tischer
Publikováno v:
Trends in Biotechnology. 17:326-335
The advantages of immobilized over soluble enzymes arise from their enhanced stability and ease of separation from the reaction media, leading to significant savings in enzyme consumption. Immobilization methods range from binding to prefabricated ca