Two GH10 endo-xylanases from Myceliophthora thermophila C1 with and without cellulose binding module act differently towards soluble and insoluble xylans.
Xylanases are mostly classified as belonging to glycoside hydrolase (GH) family 10 and 11, which differ in catalytic properties and structures. However, within one family, differences may also be present. The influence of solubility and molecular structure of substrates towards the efficiency of two GH10 xylanases from Myceliophthora thermophila C1 was investigated. The xylanases differed in degradation of high and low substituted substrate and the substitution pattern was an important factor influencing their efficiency. Alkali-labile interactions, as well as the presence of cellulose within the complex cell wall structure hindered efficient hydrolysis for both xylanases. The presence of a carbohydrate binding module did not enhance the degradation of the substrates. The differences in degradation could be related to the protein structure of the two xylanases. The study shows that the classification of enzymes does not predict their performance towards various substrates.
Laboratory of Food Chemistry, Wageningen University, P.O. Box 8129, 6700 EV Wageningen, The Netherlands.
M P
MP
van Gool
G C J
GC
van Muiswinkel
S W A
SW
Hinz
H A
HA
Schols
A P
AP
Sinitsyn
H
H
Gruppen
D001203:Ascomycota / Q000145:classification* / Q000201:enzymology*; D002482:Cellulose / Q000737:chemistry*; D043364:Endo-1,4-beta Xylanases / Q000737:chemistry*; D004789:Enzyme Activation; D004795:Enzyme Stability; D011485:Protein Binding; D012995:Solubility; D013045:Species Specificity; D014990:Xylans / Q000737:chemistry*
D014990:Xylans; D002482:Cellulose; D043364:Endo-1,4-beta Xylanases