Salinity and temperature effects on accessibility of soluble and cross-linked insoluble xylans to endo-xylanases.
Different responses to salinity were observed for an extremely halotolerant endo-xylanase when assayed with soluble birchwood glucoronoxylan and cross-linked dyed insoluble birchwood glucoronoxylan. Shrinking of insoluble xylan particles due to increased ionic strength is proposed as the explanation. Temperature affected the xylanase activity measurement on the insoluble xylan greatly, likely due to increased enzyme accessible surface of the substrate at high temperatures.
Wejse
Peter Langborg
PL
Institute of Biological Sciences, Department of Microbial Ecology, University of Aarhus, Aarhus C, Denmark.
Ingvorsen
Kjeld
K
Mortensen
Kim Kusk
KK
D043364:Endo-1,4-beta Xylanases / Q000502:physiology*; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology; D012965:Sodium Chloride; D012995:Solubility; D013379:Substrate Specificity; D013696:Temperature; D014990:Xylans / Q000378:metabolism*
D014990:Xylans; D012965:Sodium Chloride; D043364:Endo-1,4-beta Xylanases