resistance of cellulases and xylanases to proteolytic inactivation

• Published in: Applied microbiology and biotechnology Vol. 43; no. 1; pp. 52 - 57
• Main Authors: Fontes, C.M.G.A, Hall, J, Hirst, B.H, Hazlewood, G.P, Gilbert, H.J
• Format: Journal Article
• Language: English
• Published: Germany 01.04.1995
• Subjects: animal feeding; Butyrivibrio fibrisolvens; Cellulase - metabolism; cellulases; Chymotrypsin - pharmacology; Clostridium; digestive juices; duodenum; Duodenum - enzymology; enzyme activity; Escherichia coli; heat tolerance; Hot Temperature; Hydrogen-Ion Concentration; inactivation; monogastric livestock; Neocallimastix; O-glycoside hydrolases; Pancreatin - pharmacology; proteolysis; Pseudomonas fluorescens; reducing sugars; resistance; Ruminococcus albus; temperature; Xylan Endo-1,3-beta-Xylosidase; Xylosidases - metabolism

The sensitivity of a range of cellulases and xylanases to proteolytic inactivation was investigated. The xylanases, all the Clostridium thermocellum cellulases and cellulase E from Pseudomonas fluorescens subsp. cellulosa exhibited no decrease in catalytic activity during a 3-h incubation with prote...