Purification and characterization of a novel exo-beta-1,3-1,6-glucanase from the fruiting body of the edible mushroom Enoki (Flammulina velutipes).
To elucidate the role of beta-glucanases in the cell-wall degradation involved in morphogenesis, an exo-beta-1,3-1,6-glucanase (FvBGL1) was purified from fruiting bodies of the edible mushroom Enoki (Flammulina velutipes), and its enzymatic properties were studied. At least three beta-glucanases were detected in the crude extract by zymogram assay when 1% laminarin was used as substrate. The molecular mass of FvBGL1 was estimated by SDS-PAGE to be 80 kDa. The optimum pH and temperature for the action of FvBGL1 were 6.1 and 60 degrees C respectively. FvBGL1 was completely inactivated by 1 mM mercuric ions. FvBGL1 hydrolyzed F. velutipes cell-wall beta-glucan as well as beta-1,3- and beta-1,6-glucans from various sources with glucose as the only reaction product. Transglucosylation was observed when the enzyme acted on laminarinonaose. FvBGL1 can be assumed to degrade F. velutipes cell-wall beta-1,3-glucan, but most probably acts more efficiently in concert with other endogenous beta-glucan degrading enzymes.
Fukuda
Kenji
K
Meat and Milk Hygiene, Graduate School of Animal and Food Hygiene, Obihiro University of Agriculture and Veterinary Medicine, Obihiro, Hokkaido, Japan. fuku@obihiro.ac.jp
Hiraga
Michika
M
Asakuma
Sadaki
S
Arai
Ikichi
I
Sekikawa
Mitsuo
M
Urashima
Tadasu
T
D000818:Animals; D002473:Cell Wall / Q000378:metabolism; D002855:Chromatography, Thin Layer; D004792:Enzyme Precursors / Q000378:metabolism; D055393:Flammulina / Q000166:cytology / Q000201:enzymology*; D048690:Fruiting Bodies, Fungal / Q000166:cytology / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000302:isolation & purification* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D013379:Substrate Specificity
D004792:Enzyme Precursors; D006026:Glycoside Hydrolases