A novel GH6 cellobiohydrolase from Paenibacillus curdlanolyticus B-6 and its synergistic action on cellulose degradation
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Author list: Baramee S., Teeravivattanakit T., Phitsuwan P., Waeonukul R., Pason P., Tachaapaikoon C., Kosugi A., Sakka K., Ratanakhanokchai K.
Publisher: Springer
Publication year: 2017
Journal: Applied Microbiology and Biotechnology (0175-7598)
Volume number: 101
Issue number: 3
Start page: 1175
End page: 1188
Number of pages: 14
ISSN: 0175-7598
eISSN: 1432-0614
Languages: English-Great Britain (EN-GB)
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Abstract
We recently discovered a novel glycoside hydrolase family 6 (GH6) cellobiohydrolase from Paenibacillus curdlanolyticus B-6 (PcCel6A), which is rarely found in bacteria. This enzyme is a true exo-type cellobiohydrolase which exhibits high substrate specificity on amorphous cellulose and low substrate specificity on crystalline cellulose, while this showed no activity on substitution substrates, carboxymethyl cellulose and xylan, distinct from all other known GH6 cellobiohydrolases. Product profiles, HPLC analysis of the hydrolysis products and a schematic drawing of the substrate-binding subsites catalysing cellooligosaccharides can explain the new mode of action of this enzyme which prefers to hydrolyse cellopentaose. PcCel6A was not inhibited by glucose or cellobiose at concentrations up to 300 and 100 mM, respectively. A good synergistic effect for glucose production was found when PcCel6A acted together with processive endoglucanase Cel9R from Clostridium thermocellum and β-glucosidase CglT from Thermoanaerobacter brockii. These properties of PcCel6A make it a suitable candidate for industrial application in the cellulose degradation process. © 2016, Springer-Verlag Berlin Heidelberg.
Keywords
Cellobiohydrolase, Cellulose degradation, Glycoside hydrolase family 6
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