Johanna Reich
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Johanna Reich has a total of 6 co-authors. Here are the top co-authors by number of shared publications:
- Doris Ribitsch
BOKU University, Institute of Environmental Biotechnology, Department of Agricultural Sciences, Tulln an der Donau, Austria
2 shared publications - Franziska Steger
University of Natural Resources and Life Sciences Vienna, Department for Agrobiotechnology, Institute of Environmental Biotechnology, Tulln, Austria
2 shared publications - Günther Bochmann
Department IFA-Tulln, Institute of Environmental Biotechnology, University of Natural Resources and Life Sciences, Vienna, Konrad-Lorenz-Strasse 20, 3430 Tulln, Austria
2 shared publications - Simon K.-M. R. Rittmann
Archaea Physiology & Biotechnology Group, Department of Functional and Evolutionary Ecology, Universität Wien, Vienna, Austria
2 shared publications - Werner Fuchs
BOKU University, Institute of Environmental Biotechnology, Department of Agricultural Sciences, Konrad-Lorenz-Strasse 20, 3430 Tulln an der Donau, Austria
2 shared publications - Georg M. Guebitz
BOKU University, Institute of Environmental Biotechnology, Department of Agricultural Sciences, Konrad-Lorenz-Strasse 20, Tulln an der Donau, 3430, Austria
1 shared publication
Latest Publications
- Open Access
- 16 January 2022
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 23 (2) , 957
Comparison of Carbonic Anhydrases for CO2 Sequestration
Strategies for depleting carbon dioxide (CO2) from flue gases are urgently needed and carbonic anhydrases (CAs) can contribute to solving this problem. They catalyze the hydration of CO2 in aqueous solutions and therefore capture the CO2. However, the harsh conditions due to varying process temperatures are limiting factors for the application of enzymes. The current study aims to examine four recombinantly produced CAs from different organisms, namely CAs from Acetobacterium woodii (AwCA or CynT), Persephonella marina (PmCA), Methanobacterium thermoautotrophicum (MtaCA or Cab) and Sulphurihydrogenibium yellowstonense (SspCA). The highest expression yields and activities were found for AwCA (1814 WAU mg−1 AwCA) and PmCA (1748 WAU mg−1 PmCA). AwCA was highly stable in a mesophilic temperature range, whereas PmCA proved to be exceptionally thermostable. Our results indicate the potential to utilize CAs from anaerobic microorganisms to develop CO2 sequestration applications.
- 16 January 2022
- Published by MDPI AG in International Journal of Molecular Sciences
- Vol. 23 (2) , 957
Open AccessComparison of Carbonic Anhydrases for CO2 Sequestration
Strategies for depleting carbon dioxide (CO2) from flue gases are urgently needed and carbonic anhydrases (CAs) can contribute to solving this problem. They catalyze the hydration of CO2 in aqueous solutions and therefore capture the CO2. However, the harsh conditions due to varying process temperatures are limiting factors for the application of enzymes. The current study aims to examine four recombinantly produced CAs from different organisms, namely CAs from Acetobacterium woodii (AwCA or CynT), Persephonella marina (PmCA), Methanobacterium thermoautotrophicum (MtaCA or Cab) and Sulphurihydrogenibium yellowstonense (SspCA). The highest expression yields and activities were found for AwCA (1814 WAU mg−1 AwCA) and PmCA (1748 WAU mg−1 PmCA). AwCA was highly stable in a mesophilic temperature range, whereas PmCA proved to be exceptionally thermostable. Our results indicate the potential to utilize CAs from anaerobic microorganisms to develop CO2 sequestration applications.
- Open Access
A Simple and Straightforward Method for Activity Measurement of Carbonic Anhydrases
Carbonic anhydrase (CA) is an enzyme of high interest due to its high implications relative to the medical and environmental sectors. In the current paper, an enzyme assay for the determination of CA activity is proposed and it is characterized by its simplicity and high practicability. It permits the straightforward comparison of CAs performance in physiological conditions. The methodology and the theoretical background of the evaluation method are explained in detail. Moreover, the presumed advantages over alternative assays are discussed. The assay has proven to be particularly useful for the screening of CA activity with respect to their application in CO2, capturing processes for further utilization or storage.
Open AccessA Simple and Straightforward Method for Activity Measurement of Carbonic Anhydrases
Carbonic anhydrase (CA) is an enzyme of high interest due to its high implications relative to the medical and environmental sectors. In the current paper, an enzyme assay for the determination of CA activity is proposed and it is characterized by its simplicity and high practicability. It permits the straightforward comparison of CAs performance in physiological conditions. The methodology and the theoretical background of the evaluation method are explained in detail. Moreover, the presumed advantages over alternative assays are discussed. The assay has proven to be particularly useful for the screening of CA activity with respect to their application in CO2, capturing processes for further utilization or storage.