Refine
Year of publication
Institute
- Fachbereich Chemie und Biotechnologie (552) (remove)
Language
- English (552) (remove)
Document Type
- Article (473)
- Conference Proceeding (24)
- Part of a Book (18)
- Patent (17)
- Book (9)
- Conference: Meeting Abstract (8)
- Conference Poster (1)
- Preprint (1)
- Review (1)
Keywords
- Heparin (3)
- Bacillaceae (2)
- Biorefinery (2)
- Biotechnological application (2)
- Butanol (2)
- Chemometrics (2)
- IR spectroscopy (2)
- NMR spectroscopy (2)
- Principal component analysis (2)
- Standardization (2)
- Subtilases (2)
- Subtilisin (2)
- bubble column (2)
- methanation (2)
- plug flow reactor (2)
- qNMR (2)
- (Poly)saccharides (1)
- (R)- or (S)- gamma-valerolactone (1)
- 4-hydroxy valeric acid (1)
- ABE (1)
- Acid crash (1)
- Algal Turf Scrubber (1)
- Algal–bacterial bioflm (1)
- Alginate beads (1)
- Alkalihalobacillus okhensis (1)
- Aloe vera (1)
- Analytics (1)
- Authenticity (1)
- Bioeconomy (1)
- Bioethanol (1)
- Biofuel (1)
- Biogas (1)
- Biological hydrogen (1)
- Biomass (1)
- Biorefinery definitions (1)
- Bladder (1)
- Bragg peak (1)
- Broad pH spectrum (1)
- C. acetobutylicum (1)
- CRISPR/Cas9 (1)
- Carrier solvents (1)
- Chimeric liver-humanized mice (1)
- Chiralidon-R (1)
- Chiralidon-S (1)
- Chondroitin sulfate (1)
- Circular bioeconomy (1)
- Clostridium acetobutylicum (1)
- Crude heparin (1)
- Cyclotron production (1)
- Dark fermentation (1)
- Decentral (1)
- Dehydrogenase (1)
- Detergent protease (1)
- Deuterated solvents (1)
- Deuterium NMR (1)
- Diaphorase (1)
- Dietary supplements (1)
- Drug distribution (1)
- Drug metabolism (1)
- Electronic cigarettes (1)
- Enzymatic biosensor (1)
- Extracellular enzymes (1)
- Free-base nicotine (1)
- Ga-68 (1)
- Glucosamine (1)
- Growth modelling (1)
- Halotolerant protease (1)
- High-field NMR (1)
- Hydrolysis (1)
- Hypersecretion (1)
- IR (1)
- Inorganic ions (1)
- Introduction (1)
- Ions (1)
- Knockout mice (1)
- Levulinic acid (1)
- Lignocellulose (1)
- Lignocellulose feedstook (1)
- Linear discriminant analysis (1)
- Low field NMR (1)
- Manufacturer (1)
- Marker-free mutagenesis (1)
- Mechanical (1)
- Mechanical simulation (1)
- Medical radionuclide production (1)
- Metabolic shift (1)
- Metal contaminants (1)
- Methane (1)
- Microfluidic solvent extraction (1)
- Minor chemistry (1)
- Molecular modelling (1)
- Molecular weight determination (1)
- NMR (1)
- On-site (1)
- Organic acids (1)
- Organic waste (1)
- P2G (1)
- PLS-regression (1)
- Physical chemistry (1)
- Physical chemistry basics (1)
- Physical chemistry starters (1)
- Polysaccharides (1)
- Pre-culture (1)
- Pre-treatment (1)
- Pretreatment (1)
- Process schemes (1)
- Quality control (1)
- Quantum chemistry (1)
- Reconstruction (1)
- Renewable resources (1)
- Simultaneous determination (1)
- Soft independent modeling of class analogy (1)
- Spectroscopy (1)
- Stenotrophomonas maltophilia (1)
- Streptomyces griseus (1)
- Streptomyces lividans (1)
- Thermodynamics as minor (1)
- Toxicology (1)
- USP (1)
- Uracil-phosphoribosyltransferase (1)
- Ureter (1)
- Weak organic acids (1)
- acetoin (1)
- acetoin reductase (1)
- actuator-sensor system (1)
- alcoholic beverages (1)
- aspergillus (1)
- bacterial cellulose (1)
- bi-enzyme biosensor (1)
- bio-methane (1)
- bioavailability (1)
- biodegradable polymers (1)
- biological dosimeter (1)
- biomethane (1)
- biosensors (1)
- borehole disposal (1)
- capacitive field-effect sensor (1)
- capacitive field-effect sensors (1)
- coculture (1)
- deficit irrigation (1)
- detergent protease (1)
- disposal facility (1)
- drug metabolising enzymes (1)
- drug–drug interactions (1)
- elastomers (1)
- enzyme kinetics (1)
- enzyme-logic gate (1)
- exopolysaccharides (1)
- fatty acid (1)
- filamentous fungi (1)
- genome engineering (1)
- geological disposal (1)
- glycine (1)
- halotolerant protease (1)
- high-alkaline subtilisin (1)
- human metabolites (1)
- hydrogel (1)
- hydrogels (1)
- light-addressable electrode (1)
- light-addressable potentiometric sensor (1)
- mechanical properties (1)
- metathesis (1)
- microfluidics (1)
- micronutrients (1)
- neutrons (1)
- nuclear waste (1)
- onion (1)
- optical fibers (1)
- oxidative stable protease (1)
- penicillinase (1)
- polyamide (1)
- polyaspartic acid (1)
- polyester (1)
- power-to-gas (1)
- prebiotic (1)
- proton therapy (1)
- protons (1)
- pullulan (1)
- recombinant expression (1)
- relative dosimetry (1)
- renewable resources (1)
- retention time (1)
- rubber (1)
- superabsorbent polymers (1)
- supramolecular structures (1)
- swelling properties (1)
- theory and modeling (1)
- tobacco mosaic virus (TMV) (1)
- transporters (1)
- urease (1)
- water economy (1)
- yield (1)
- α-aminoacylase (1)
- ε-lysine acylase (1)
Bacillus pumilus reveals a remarkably high resistance to hydrogen peroxide provoked oxidative stress
(2014)
Bacillus pumilus is characterized by a higher oxidative stress resistance than other comparable industrially relevant Bacilli such as B. subtilis or B. licheniformis. In this study the response of B. pumilus to oxidative stress was investigated during a treatment with high concentrations of hydrogen peroxide at the proteome, transcriptome and metabolome level. Genes/proteins belonging to regulons, which are known to have important functions in the oxidative stress response of other organisms, were found to be upregulated, such as the Fur, Spx, SOS or CtsR regulon. Strikingly, parts of the fundamental PerR regulon responding to peroxide stress in B. subtilis are not encoded in the B. pumilus genome. Thus, B. pumilus misses the catalase KatA, the DNA-protection protein MrgA or the alkyl hydroperoxide reductase AhpCF. Data of this study suggests that the catalase KatX2 takes over the function of the missing KatA in the oxidative stress response of B. pumilus. The genome-wide expression analysis revealed an induction of bacillithiol (Cys-GlcN-malate, BSH) relevant genes. An analysis of the intracellular metabolites detected high intracellular levels of this protective metabolite, which indicates the importance of bacillithiol in the peroxide stress resistance of B. pumilus.
Lignin is a promising renewable biopolymer being investigated worldwide as an environmentally benign substitute of fossil-based aromatic compounds, e.g. for the use as an excipient with antioxidant and antimicrobial properties in drug delivery or even as active compound. For its successful implementation into process streams, a quick, easy, and reliable method is needed for its molecular weight determination. Here we present a method using 1H spectra of benchtop as well as conventional NMR systems in combination with multivariate data analysis, to determine lignin’s molecular weight (Mw and Mn) and polydispersity index (PDI). A set of 36 organosolv lignin samples (from Miscanthus x giganteus, Paulownia tomentosa and Silphium perfoliatum) was used for the calibration and cross validation, and 17 samples were used as external validation set. Validation errors between 5.6% and 12.9% were achieved for all parameters on all NMR devices (43, 60, 500 and 600 MHz). Surprisingly, no significant difference in the performance of the benchtop and high-field devices was found. This facilitates the application of this method for determining lignin’s molecular weight in an industrial environment because of the low maintenance expenditure, small footprint, ruggedness, and low cost of permanent magnet benchtop NMR systems.
Bio-feedstocks
(2011)
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.
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.