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...

Full description

Saved in:
Bibliographic Details
Published inApplied 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
LanguageEnglish
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
Online AccessGet more information

Cover

More Information
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