resistance of cellulases and xylanases to proteolytic inactivation

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...

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Bibliographic Details
Published in:Applied microbiology and biotechnology 1995-04, Vol.43 (1), p.52-57
Main Authors: Fontes, C.M.G.A, Hall, J, Hirst, B.H, Hazlewood, G.P, Gilbert, H.J
Format: Article
Language:English
Subjects:
animal feeding
Biological and medical sciences
Biotechnology
Butyrivibrio fibrisolvens
Cellulase - metabolism
cellulases
Chymotrypsin - pharmacology
Clostridium
Clostridium thermocellum
digestive juices
duodenum
Duodenum - enzymology
enzyme activity
Enzyme engineering
Escherichia coli
Fundamental and applied biological sciences. Psychology
heat tolerance
Hot Temperature
Hydrogen-Ion Concentration
inactivation
Methods. Procedures. Technologies
Miscellaneous
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
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Summary: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 proteinases of the small intestine. Under these conditions, the control Escherichia coli enzymes analysed had half-lives of 4.3-13.5 min. The addition of substrate significantly decreased the sensitivity of proteinase-labile enzymes to inactivation. The significance of these data in relation to the use of cellulases and xylanases for improving animal nutrition is discussed.
ISSN:0175-7598
1432-0614
DOI:10.1007/BF00170622