Characterization of Fusarium oxysporum beta-1,6-galactanase, an enzyme that hydrolyzes larch wood arabinogalactan.
A type II arabinogalactan-degrading enzyme (FoGal1) was purified from Fusarium oxysporum 12S, and the corresponding cDNA was isolated. FoGal1 had high similarity to enzymes of glycoside hydrolase family 5. Treatment of larch wood arabinogalactan with the recombinant enzyme indicated that FoGal1 is a beta-1,6-galactanase that preferentially debranches beta-1,6-galactobiose from the substrate.
Sakamoto
Tatsuji
T
Division of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Osaka 599-8531, Japan. sakamoto@biochem.osakafu-u.ac.jp
Taniguchi
Yuya
Y
Suzuki
Shiho
S
Ihara
Hideshi
H
Kawasaki
Haruhiko
H
D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D005670:Fusarium / Q000201:enzymology*; D005685:Galactans / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D028221:Larix / Q000737:chemistry; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D017422:Sequence Analysis, DNA; D013696:Temperature; D001616:beta-Galactosidase / Q000737:chemistry* / Q000378:metabolism
D005656:Fungal Proteins; D005685:Galactans; D011994:Recombinant Proteins; D001616:beta-Galactosidase; C005653:arabinogalactan