TY - JOUR A1 - Darmo, J. A1 - Schäffer, F. A1 - Förster, Arnold A1 - Kordos, P. T1 - Beryllium doped low-temperature-grown MBE GaAs: material for photomixing in the THz frequency range JF - ASDAM 2000 : conference proceedings / edited by Jozef Osvald ... [et al.] Y1 - 2000 SN - 0780359399 N1 - International Conference on Advanced Semiconductor Devices and Microsystems ; (3rd : ; 2000 : ; Smolenice, Slovakia) SP - 147 EP - 150 PB - IEEE CY - Piscataway, NJ ER - TY - JOUR A1 - Kramer, Friederike A1 - Halamkova, Lenka A1 - Poghossian, Arshak A1 - Schöning, Michael Josef A1 - Katz, Evgeny A1 - Halamek, Jan T1 - Biocatalytic analysis of biomarkers for forensic identification of ethnicity between Caucasian and African American JF - The analyst. August 2013 Y1 - 2013 SN - 1364-5528 (E-Journal); 0003-2654 (Print) VL - Vol. 138 SP - 6251 EP - 6257 PB - Royal Society of Chemistry CY - Cambridge ER - TY - JOUR A1 - Falkenberg, Fabian A1 - Kohn, Sophie A1 - Bott, Michael A1 - Bongaerts, Johannes A1 - Siegert, Petra T1 - Biochemical characterisation of a novel broad pH spectrum subtilisin from Fictibacillus arsenicus DSM 15822ᵀ JF - FEBS Open Bio N2 - Subtilisins from microbial sources, especially from the Bacillaceae family, are of particular interest for biotechnological applications and serve the currently growing enzyme market as efficient and novel biocatalysts. Biotechnological applications include use in detergents, cosmetics, leather processing, wastewater treatment and pharmaceuticals. To identify a possible candidate for the enzyme market, here we cloned the gene of the subtilisin SPFA from Fictibacillus arsenicus DSM 15822ᵀ (obtained through a data mining-based search) and expressed it in Bacillus subtilis DB104. After production and purification, the protease showed a molecular mass of 27.57 kDa and a pI of 5.8. SPFA displayed hydrolytic activity at a temperature optimum of 80 °C and a very broad pH optimum between 8.5 and 11.5, with high activity up to pH 12.5. SPFA displayed no NaCl dependence but a high NaCl tolerance, with decreasing activity up to concentrations of 5 m NaCl. The stability enhanced with increasing NaCl concentration. Based on its substrate preference for 10 synthetic peptide 4-nitroanilide substrates with three or four amino acids and its phylogenetic classification, SPFA can be assigned to the subgroup of true subtilisins. Moreover, SPFA exhibited high tolerance to 5% (w/v) SDS and 5% H₂O₂ (v/v). The biochemical properties of SPFA, especially its tolerance of remarkably high pH, SDS and H₂O₂, suggest it has potential for biotechnological applications. KW - Bacillaceae KW - Biotechnological application KW - Broad pH spectrum KW - Subtilases KW - Subtilisin Y1 - 2023 U6 - http://dx.doi.org/10.1002/2211-5463.13701 SN - 2211-5463 N1 - Corresponding author: Petra Siegert VL - 13 IS - 11 SP - 2035 EP - 2046 PB - Wiley CY - Hoboken, NJ ER - TY - JOUR A1 - Falkenberg, Fabian A1 - Rahba, Jade A1 - Fischer, David A1 - Bott, Michael A1 - Bongaerts, Johannes A1 - Siegert, Petra T1 - Biochemical characterization of a novel oxidatively stable, halotolerant, and high-alkaline subtilisin from Alkalihalobacillus okhensis Kh10-101T JF - FEBS Open Bio N2 - Halophilic and halotolerant microorganisms represent a promising source of salt-tolerant enzymes suitable for various biotechnological applications where high salt concentrations would otherwise limit enzymatic activity. Considering the current growing enzyme market and the need for more efficient and new biocatalysts, the present study aimed at the characterization of a high-alkaline subtilisin from Alkalihalobacillus okhensis Kh10-101T. The protease gene was cloned and expressed in Bacillus subtilis DB104. The recombinant protease SPAO with 269 amino acids belongs to the subfamily of high-alkaline subtilisins. The biochemical characteristics of purified SPAO were analyzed in comparison with subtilisin Carlsberg, Savinase, and BPN'. SPAO, a monomer with a molecular mass of 27.1 kDa, was active over a wide range of pH 6.0–12.0 and temperature 20–80 °C, optimally at pH 9.0–9.5 and 55 °C. The protease is highly oxidatively stable to hydrogen peroxide and retained 58% of residual activity when incubated at 10 °C with 5% (v/v) H2O2 for 1 h while stimulated at 1% (v/v) H2O2. Furthermore, SPAO was very stable and active at NaCl concentrations up to 5.0 m. This study demonstrates the potential of SPAO for biotechnological applications in the future. KW - Alkalihalobacillus okhensis KW - detergent protease KW - halotolerant protease KW - high-alkaline subtilisin KW - oxidative stable protease Y1 - 2022 U6 - http://dx.doi.org/10.1002/2211-5463.13457 SN - 2211-5463 N1 - Corresponding author: Petra Siegert VL - 12 IS - 10 SP - 1729 EP - 1746 PB - Wiley CY - Hoboken, NJ ER - TY - JOUR A1 - Lüth, H. A1 - Thust, M. A1 - Steffen, A. A1 - Kordos, P. A1 - Schöning, Michael Josef T1 - Biochemical sensors with structured and porous silicon capacitors JF - Materials Science and Engineering B. 69-70 (2000) Y1 - 2000 SN - 0921-5107 SP - 104 EP - 108 ER - TY - JOUR A1 - Schroth, P. A1 - Weißbecker, B. A1 - Schütz, S. A1 - Ecken, H. A1 - Yoshinobu, T. A1 - Lüth, H. A1 - Schöning, Michael Josef T1 - Bioelectronic signal processing - intact chemoreceptors coupled to field-effect devices JF - Lecture Notes of the ICB Seminars Y1 - 2002 SP - 28 EP - 42 PB - MCB CY - Warsaw ER - TY - JOUR A1 - Schroth, P. A1 - Weißbecker, B. A1 - Schütz, S. A1 - Ecken, H. A1 - Yoshinobu, T. A1 - Lüth, H. A1 - Schöning, Michael Josef T1 - Bioelectronic signal processing - intact chemoreceptors coupled to field-effect devices JF - Biocybernetics and Biomedical Engineering. 21 (2001), H. 3 Y1 - 2001 SN - 0208-5216 SP - 27 EP - 42 ER - TY - JOUR A1 - Schöning, Michael Josef A1 - Poghossian, Arshak T1 - BioFEDs (field-effect devices) : State-of-the-art and new directions JF - Electroanalysis Y1 - 2006 U6 - http://dx.doi.org/10.1002/elan.200603609 SN - 1521-4109 VL - 18 IS - 19-20 SP - 1893 EP - 1900 ER - TY - CHAP A1 - Kasper, Katharina A1 - Schiffels, Johannes A1 - Krafft, Simone A1 - Kuperjans, Isabel A1 - Elbers, Gereon A1 - Selmer, Thorsten T1 - Biogas Production on Demand Regulated by Butyric Acid Addition T2 - IOP Conference Series: Earth and Environmental Science. Bd. 32 Y1 - 2016 U6 - http://dx.doi.org/10.1088/1755-1315/32/1/012009 SN - 1755-1315 N1 - ICARET 2016, International Conference on Advances in Renewable Energy and Technologies, Putrajaya, MY, Feb 23-25, 2016 VL - 32 SP - 012009/1 EP - 012009/4 ER - TY - JOUR A1 - Oliveira, Danilo A. A1 - Molinnus, Denise A1 - Beging, Stefan A1 - Siqueira Jr, José R. A1 - Schöning, Michael Josef T1 - Biosensor Based on Self-Assembled Films of Graphene Oxide and Polyaniline Using a Field-Effect Device Platform JF - physica status solidi (a) applications and materials science N2 - A new functionalization method to modify capacitive electrolyte–insulator–semiconductor (EIS) structures with nanofilms is presented. Layers of polyallylamine hydrochloride (PAH) and graphene oxide (GO) with the compound polyaniline:poly(2-acrylamido-2-methyl-1-propanesulfonic acid) (PANI:PAAMPSA) are deposited onto a p-Si/SiO2 chip using the layer-by-layer technique (LbL). Two different enzymes (urease and penicillinase) are separately immobilized on top of a five-bilayer stack of the PAH:GO/PANI:PAAMPSA-modified EIS chip, forming a biosensor for detection of urea and penicillin, respectively. Electrochemical characterization is performed by constant capacitance (ConCap) measurements, and the film morphology is characterized by atomic force microscopy (AFM) and scanning electron microscopy (SEM). An increase in the average sensitivity of the modified biosensors (EIS–nanofilm–enzyme) of around 15% is found in relation to sensors, only carrying the enzyme but without the nanofilm (EIS–enzyme). In this sense, the nanofilm acts as a stable bioreceptor onto the EIS chip improving the output signal in terms of sensitivity and stability. KW - capacitive electrolyte–insulator–semiconductor sensors KW - graphene oxide KW - layer-by-layer technique KW - nanomaterials KW - polyaniline Y1 - 2021 U6 - http://dx.doi.org/10.1002/pssa.202000747 SN - 1862-6319 N1 - Corresponding author: José R. Siqueira Jr & Michael J. Schöning VL - 218 IS - 13 SP - 1 EP - 9 PB - Wiley-VCH CY - Weinheim ER -