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 - Selmer, Thorsten A1 - Netz, Daili Jacqueline Aguilar A1 - Pohl, Regula A1 - Beck-Sickinger, Annette G. T1 - Biochemical characterisation and genetic analysis of aureocin A53, a new, atypical bacteriocin from Staphylococcus aureus / Netz, Daili Jacqueline Aguilar ; Pohl, Regula ; Beck-Sickinger, Annette G. ; Selmer, Thorsten ; Pierik, Antonio J. ; Carmo de Frei JF - Journal of Molecular Biology. 319 (2002), H. 3 Y1 - 2002 SN - 0022-2836 SP - 745 EP - 756 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 - Akimbekov, N. S. A1 - Digel, Ilya A1 - Tastambek, K. T. A1 - Zhubanova, A. A. T1 - Biocompatibility of carbonized rice husk with a rat heart cells line H9c2 JF - Experimental Biology Y1 - 2013 SN - 1563-0218 N1 - Original in russischer Sprache VL - 59 IS - 3/1 SP - 23 EP - 25 ER - TY - CHAP A1 - Mansurov, Zulkhair A. A1 - Jandosov, Jakpar A1 - Chenchik, D. A1 - Azat, Seitkhan A1 - Savitskaya, Irina S. A1 - Kistaubaeva, Aida A1 - Akimbekov, Nuraly A1 - Digel, Ilya A1 - Zhubanova, Azhar Achmet T1 - Biocomposite Materials Based on Carbonized Rice Husk in Biomedicine and Environmental Applications T2 - Carbon Nanomaterials in Biomedicine and the Environment N2 - This chapter describes the prospects for biomedical and environmental engineering applications of heterogeneous materials based on nanostructured carbonized rice husk. Efforts in engineering enzymology are focused on the following directions: development and optimization of immobilization methods leading to novel biotechnological and biomedical applications; construction of biocomposite materials based on individual enzymes, multi-enzyme complexes and whole cells, targeted on realization of specific industrial processes. Molecular biological and biochemical studies on cell adhesion focus predominantly on identification, isolation and structural analysis of attachment-responsible biological molecules and their genetic determinants. The chapter provides a short overview of applications of the biocomposite materials based of nanostructured carbonized adsorbents. It emphasizes that further studies and better understanding of the interactions between CNS and microbial cells are necessary. The future use of living cells as biocatalysts, especially in the environmental field, needs more systematic investigations of the microbial adsorption phenomenon. Y1 - 2020 SN - 978-981-4800-27-3 U6 - http://dx.doi.org/10.1201/9780429428647-2 SP - 3 EP - 32 PB - Jenny Stanford Publishing Pte. Ltd. CY - Singapore 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 - BOOK A1 - Artmann, Gerhard T1 - Bioengineering in Cell and Tissue Research / Artmann, Gerhard M. ; Chien, Shu (Eds.) Y1 - 2008 SN - 978-3-540-75408-4 PB - Springer CY - Berlin ER -