Publikation: Characterization of pectinolytic enzymes of Clostridium thermosulfurogenes
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Pectinolytic activity is of general importance to the degradation of organic matter in the biosphere and as a biochemical agent of plant spoilage or pathogenesis [1-4]. Certain types of pectinolytic enzymes are vendable and of significance to agricultural and food processing [1,2]. Enzymes from thermophilic bacteria often possess higher catalytic activity and stability than
those of mesophilic microorganisms [5]. Nonetheless, only recently has a polygalacturonate lyase (EC 4.2.2.10) been characterized from the caldoacrive bacterium, Bacillus stearothermophilus [6]. We recently isolated and described the properties of Clostridium thermosulfurogenes that was obtained from Yellowstone National Park, U.S.A. [7]. This species was novel because it transformed thiosulfate into elemental sulfur which accumulated in the medium and cells and because it proliferated with a doubling time of 2 h on glucose as well as pectin. However, the general enzymatic features of the pectinolytic activity displayed by this new species were not described. This communication shows that C. thermosulfurogenes produces an active thermostable polygalacturonate hydrolase (EC 3.2.1.15) and pectin methylesterase (EC 3.1.1.11).
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SCHINK, Bernhard, J. Gregory ZEIKUS, 1983. Characterization of pectinolytic enzymes of Clostridium thermosulfurogenes. In: FEMS Microbiology letters. 1983, 17(1-3), pp. 295-298. ISSN 0378-1097. eISSN 1574-6968. Available under: doi: 10.1111/j.1574-6968.1983.tb00422.xBibTex
@article{Schink1983Chara-8221, year={1983}, doi={10.1111/j.1574-6968.1983.tb00422.x}, title={Characterization of pectinolytic enzymes of Clostridium thermosulfurogenes}, number={1-3}, volume={17}, issn={0378-1097}, journal={FEMS Microbiology letters}, pages={295--298}, author={Schink, Bernhard and Zeikus, J. Gregory} }
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