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Treffer 1-10 von 30 (Suchzeit: 0.004 Sekunden).
Treffer Dokumente:
ErscheinungsdatumTitelAutor(en)
2006Reconstitution of beta-carotene hydroxylase activity of thermostable CYP175A1 monooxygenaseMomoi, Kyoko; Hofmann, Ute; Schmid, Rolf D.; Urlacher, Vlada B.
2003Identification of factors impeding the production of a single-chain antibody fragment in Escherichia coli by comparing in vivo and in vitro expressionÖlschläger, Peter; Lange, Stefan; Schmitt, Jutta; Siemann-Herzberg, Martin; Reuss, Matthias; Schmid, Rolf D.
2002Rapid detection of neurotoxic insecticides in food using disposable acetylcholinesterase-biosensors and simple solvent extractionSchulze, Holger; Schmid, Rolf D.; Bachmann, Till T.
2002Development, validation, and application of an acetylcholinesterase-biosensor test for the direct detection of insecticide residues in infant foodSchulze, Holger; Scherbaum, Ellen; Anastassiades, Michelangelo; Vorlová, Sandra; Schmid, Rolf D.; Bachmann, Till T.
2003Directed evolution of a bacterial alpha-amylase : towards enhanced pH-performance and higher specific activityBessler, Cornelius; Schmitt, Jutta; Maurer, Karl-Heinz; Schmid, Rolf D.
2002Blocking the tunnel: engineering of Candida rugosa lipase mutants with short chain length specificitySchmitt, Jutta; Brocca, Stefania; Schmid, Rolf D.; Pleiss, Jürgen
2003Immobilisation of P450 BM-3 and an NADP+ cofactor recycling system : towards a technical application of heme-containing monooxygenases in fine chemical synthesisMaurer, Steffen Christian; Schulze, Holger; Schmid, Rolf D.; Urlacher, Vlada B.
2001Structural basis of stereoselectivity in Candida rugosa lipase-catalyzed hydrolysis of secondary alcoholsSchulz, Tanja; Schmid, Rolf D.; Pleiss, Jürgen
2003Insight into the mechanism of the IMP-1 metallo-beta-lactamase by molecular dynamics simulationsÖlschläger, Peter; Schmid, Rolf D.; Pleiss, Jürgen
2006Cloning, expression, and characterization of a self-sufficient cytochrome P450 monooxygenase from Rhodococcus ruber DSM 44319Liu, Luo; Schmid, Rolf D.; Urlacher, Vlada B.