The N-terminal family 22 carbohydrate-binding module of xylanase 10B of Clostridium themocellum is not a thermostabilizing domain |
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Authors: | Dias Fernando M V Goyal Arun Gilbert Harry J José A M Prates Ferreira Luís M A Fontes Carlos M G A |
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Institution: | Universidade Técnica de Lisboa, CIISA--Faculdade de Medicina Veterinária, Rua Prof. Cid dos Santos, 1300-477 Lisboa, Portugal. |
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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. |
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Keywords: | Xylanase Carbohydrate-binding module Resistance to thermoinactivation Glycoside hydrolase Thermostability Clostridium thermocellum |
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