Purification, molecular cloning, and enzymatic properties of a family 12 endoglucanase (EG-II) from fomitopsis palustris: role of EG-II in larch holocellulose hydrolysis.
A family 12 endoglucanase with a molecular mass of 23,926 Da (EG-II) from the brown-rot basidiomycete Fomitopsis palustris was purified and characterized. One of the roles of EG-II in wood degradation is thought to be to loosen the polysaccharide network in cell walls by disentangling hemicelluloses that are associated with cellulose.
Shimokawa
Tomoko
T
Forestry and Forest Products Research Institute, Matsunosato 1, Tsukuba, Ibaraki 305-8687, Japan. tshimo@ffpri.affrc.go.jp
Shibuya
Hajime
H
Nojiri
Masanobu
M
Yoshida
Shigeki
S
Ishihara
Mitsuro
M
D002480:Cellulase / Q000235:genetics*; D002482:Cellulose / Q000378:metabolism*; D003001:Cloning, Molecular; D005800:Genes, Fungal; D006868:Hydrolysis; D028221:Larix / Q000382:microbiology; D008969:Molecular Sequence Data; D020072:Polyporales / Q000201:enzymology* / Q000235:genetics* / Q000378:metabolism; D012331:RNA, Fungal / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013379:Substrate Specificity; D014934:Wood / Q000378:metabolism
D012331:RNA, Fungal; D002482:Cellulose; C056373:endoglucanase 2; D002480:Cellulase