Jonathan Caspi
Weizmann Institute of Science
14 Papers
162 Citations
Jonathan Caspi is an academic researcher from Weizmann Institute of Science. The author has contributed to research in topics: Dockerin & Cellulosome. The author has an hindex of 10, co-authored 10 publications.
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Papers
Cellulase-Xylanase Synergy in Designer Cellulosomes for Enhanced Degradation of a Complex Cellulosic Substrate
Sarah Moraïs,Sarah Moraïs,Yoav Barak,Jonathan Caspi,Yitzhak Hadar,Raphael Lamed,Yuval Shoham,David Wilson,Edward A. Bayer +8 more
TL;DR: Results provide additional evidence that close proximity between cellulases and xylanases is key to the observed concerted degradation of the complex cellulosic substrate in which the integrated enzymes complement each other by promoting access to the relevant polysaccharide components of the substrate.
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Distribution of split DnaE inteins in cyanobacteria
TL;DR: The hypothesis, findings and the cloning procedure that is established allow the identification and acquisition of many naturally split inteins and suggest the occurrence of a genetic rearrangement in the ancestor of a large division of cyanobacteria.
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Effect of Linker Length and Dockerin Position on Conversion of a Thermobifida fusca Endoglucanase to the Cellulosomal Mode
Jonathan Caspi,Yoav Barak,Rachel Haimovitz,Diana C. Irwin,Raphael Lamed,David Wilson,Edward A. Bayer +6 more
TL;DR: The results demonstrated that cellulose binding played a major role in the degradation of crystalline cellulosic substrates and promote the development of more complex multienzyme designer cellulosomes, which may eventually be applied for improved degradation of plant cell wall biomass.
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Conversion of Thermobifida fusca free exoglucanases into cellulosomal components: Comparative impact on cellulose-degrading activity
Jonathan Caspi,Diana C. Irwin,Raphael Lamed,Yongchao Li,Henri-Pierre Fierobe,David Wilson,Edward A. Bayer +6 more
TL;DR: The marked difference in the response of the two exoglucanases to incorporation into a cellulosome, suggests that thefamily-48 cellulase is more appropriate than the family-6 enzyme as a designer cellulosomes component.
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Contribution of a xylan-binding module to the degradation of a complex cellulosic substrate by designer cellulosomes.
Sarah Moraïs,Yoav Barak,Jonathan Caspi,Yitzhak Hadar,Raphael Lamed,Yuval Shoham,David Wilson,Edward A. Bayer +7 more
TL;DR: The conversion of the T. fusca xylanases Xyn11A and Xyn10B and their synergistic interaction in the free state or within designer cellulosome complexes in order to enhance specific degradation of hatched wheat straw as a model for a complex cellulosic substrate is described.
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