K
Karin Bronnenmeier
Researcher at Technische Universität München
Publications - 27
Citations - 1576
Karin Bronnenmeier is an academic researcher from Technische Universität München. The author has contributed to research in topics: Clostridium stercorarium & Cellulase. The author has an hindex of 21, co-authored 27 publications receiving 1515 citations.
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Activity staining of cellulases in polyacrylamide gels containing mixed linkage beta-glucans.
TL;DR: Endoglucanase and cellobiohydrolase components of thermophilic cellulases can be detected in situ after gel electrophoresis in the presence of sodium dodecyl sulfate by incorporating a mixed linkage beta-glucan (barley beta- glucan, lichenan) in the separation gel.
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Properties and gene structure of a bifunctional cellulolytic enzyme (CelA) from the extreme thermophile ‘Anaerocellum thermophilum’ with separate glycosyl hydrolase family 9 and 48 catalytic domains
TL;DR: The CelA-encoding gene encodes a protein of 1711 amino acids starting with the sequence found at the N-terminus of CelA purified from 'Anaerocellum thermophilum', and exoglucanase activity may be ascribed to the C-terminal family 48 catalytic domain.
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Purification of Thermotoga maritima enzymes for the degradation of cellulosic materials.
TL;DR: A separation procedure for the analysis of the enzyme components of the hyperthermophilic bacterium Thermotoga maritima involved in cellulose and xylan degradation was developed by a combination of fast protein liquid chromatography anion exchange and hydrophobic interaction chromatography.
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The thermostable alpha-L-rhamnosidase RamA of Clostridium stercorarium: biochemical characterization and primary structure of a bacterial alpha-L-rhamnoside hydrolase, a new type of inverting glycoside hydrolase.
Vladimir V. Zverlov,Christian Hertel,Karin Bronnenmeier,Angelika Hroch,Josef Kellermann,Wolfgang H. Schwarz +5 more
TL;DR: An α‐l‐rhamnosidase clone was isolated from a genomic library of the thermophilic anaerobic bacterium Clostridium stercorarium and its primary structure was determined, indicating a single displacement mechanism.
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Analysis of a Thermotoga maritima DNA fragment encoding two similar thermostable cellulases, CelA and CelB, and characterization of the recombinant enzymes
Wolfgang Liebl,Peter Ruile,Karin Bronnenmeier,Katrin Riedel,Friedrich Lottspeich,Ingrid Greif +5 more
TL;DR: Recombinant Escherichia coli clones displaying thermostable beta-glucanase activity were isolated from two different gene libraries of the hyperthermophilic bacterium Thermotoga maritima MSB8, and the nucleotide sequence of a 1,4-beta-glUCanase gene designated celA was determined.