Ma, Kesen - University of Waterloo - Department of Biology

个人简介

Kesen Ma carries out research in physiology and enzymology of hyperthermophiles, a group of microorganisms growing at temperatures of boiling water. Metabolic processes involved in the conversion of biomass to biofuels and bioproducts at elevated temperatures are studied. Novel thermostable enzymes functioning in these processes are identified and characterized. His research provides further understanding of the mechanisms of protein thermostability, unusual metabolic pathways and biocatalysis at high temperatures, and also explores potential applications of these biocatalysts in pharmaceutical and other industrial processes. Microbiology Biochemistry and enzymology Protein purification and analysis Metal-containing proteins Microbial physiology Fermentation Molecular biology Hyperthermophiles Canadian Society of Microbiologists American Society for Microbiology International Society for Extremophiles Canadian Society for Molecular BioSciences 1989 PhD Microbial Biochemistry, Philipps-Universitat Marburg 1984 MSc Microbiology, Academia Sinica 1982 BSc Microbiology, Wuhan University

研究领域

Physiology and enzymology of hyperthermophilic microorganisms. Current research interests: sulfur reduction and energy metabolism; thermostable dehydrogenases; alcohol metabolism; electron transfer and flavoproteins; enzyme evolution and protein engineering. Hyperthermophiles are a group of microorganisms isolated mainly from deep sea hydrothermal vents and capable of growing at temperatures of ³ 90°C. The majority of hyperthermophiles are classified as Archaea that are considered as the most slowly evolving of all microorganisms. The metabolism at such high temperature (>100°C) raises many biochemical questions: how are biomolecules stabilized? are there new metabolic pathways and novel metabolites? do these pathways contain unusual enzymes with yet unknown catalytic mechanisms? what is the relationship between structure and function of biomolecules that evolved under extreme conditions? Answering these questions will provide valuable insight into high temperature biochemistry and protein engineering. Novel enzymes are involved in alcohol fermentation at high temperatures, which include both alcohol dehydrogenase and pyruvate decarboxylase. It is particularly interesting to characterize new types of acetaldehyde-producing enzymes from hyperthermophiles. This research will provide further information required for developing a more efficient system for alcohol fermentation at high temperatures.

近期论文

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Eram, M.S., and K. Ma. 2016. Pyruvate decarboxylase activity of the acetohydroxyacid synthase of Thermotoga maritima. BBREP. (2016), pp. 394-399. doi:10.1016/j.bbrep.2016.07.008 Eram, M.S., B. Sarafuddin, F. Gong, K. Ma. 2015. Characterization of acetohydroxyacid synthase from the hyperthermophilic bacterium Thermotoga maritima. BBREP. 4:89-97 DOI: 10.1016/j.bbrep.2015.08. 014 Yang, X., L. Hao, H. Zhu, and K. Ma. 2015. Purification and Molecular Characterization of an [FeFe]-Hydrogenase from Thermotoga hypogea. Curr. Biotechnol. 4:118-127 Eram, M.S., E. Oduaran, and K. Ma. 2014. The Bifunctional Pyruvate Decarboxylase/Pyruvate Ferredoxin Oxidoreductase from Thermococcus guaymasensis. Archaea. 2014: Article ID 349379, 13 pages. doi:10.1155/2014/349379 Dhanjoon, J., X. Ying, F. Salma, and K. Ma. 2013. Characterization of a Thermostable Xylanase from the Extremely Thermophilic Bacterium Thermotoga hypogea. Current Biotechnology. 2:325-333 Eram, M. S. and K. Ma. 2013. Decarboxylation of Pyruvate to Acetaldehyde for Ethanol Production by Hyperthermophiles. Biomolecules. 3:578-596; doi:10.3390/biom3030578 Ying, X and Ma, K. 2011. Characterization of a Zinc-containing Alcohol Dehydrogenase with Stereoselectivity from Hyperthermophilic Archaeon Thermococcus guaymasensis. J. Bacteriol. 193:3009-3019. Yang, X. and K. Ma. 2010. Characterization of a thioredoxin-thioredoxin reductase system from the hyperthermophilic bacterium Thermotoga maritima. J. Bacteriol. 192: 1370–1376.