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- W2077182480 abstract "Xylanase Xyn10B from Clostridium thermocellum is a modular enzyme that contains two family 22 carbohydrate binding modules N- (CBM22-1) and C- (CBM22-2) terminal of the family 10 glycoside hydrolase catalytic domain (GH10). In a previous study, we showed that removal of CBM22-1 reduces the resistance to thermoinactivation of the enzyme suggesting that this module is a thermostabilizing domain. Here, we show that it is the module border on the N-terminal side of GH10 that confers resistance to thermoinactivation and to proteolysis. Therefore, CBM22-1 does not function as a thermostabilizing domain and the role for this apparently non-functional CBM remains elusive." @default.
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- W2077182480 date "2004-09-01" @default.
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- W2077182480 title "The N-terminal family 22 carbohydrate-binding module of xylanase 10B of is not a thermostabilizing domain" @default.
- W2077182480 doi "https://doi.org/10.1016/j.femsle.2004.07.019" @default.
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