Purification and Some Properties of a New Levanase from Bacillus sp. No. 71.
A levanase from Bacillus sp. was purified to a homogeneous state. The enzyme had a molecular weight of 135,000 and an isoelectric point of pH 4.7. The enzyme was most active at pH 6.0 and 40°C, stable from pH 6.0 to 10.0 for 20 hr of incubation at 4°C and up to 30°C for 30 min of incubation at pH 6.0. The enzyme activity was inhibited by Ag (+), Hg(2 +), Cu(2 +), Fe(3 +), Pb(2+), and p-chloromercuribenzoic acid. The enzyme hydrolyzed levan and phlein endowise to produce levanheptaose as a main product. The limit of hydrolysis of levan and phlein were 71% and 96%, respectively.
a Osaka Municipal Technical Research Institute, 6-50 Morinomiya 1-chome, Jyoto-ku , Osaka 536 , Japan.
H
H
Murakami
a Osaka Municipal Technical Research Institute, 6-50 Morinomiya 1-chome, Jyoto-ku , Osaka 536 , Japan.|b Maruzen Kasei Co., Ltd., 14703-10 Mukaihigashi-cho , Onomichi-shi 722 , Japan.
T
T
Kuramoto
a Osaka Municipal Technical Research Institute, 6-50 Morinomiya 1-chome, Jyoto-ku , Osaka 536 , Japan.|b Maruzen Kasei Co., Ltd., 14703-10 Mukaihigashi-cho , Onomichi-shi 722 , Japan.
K
K
Mizutani
a Osaka Municipal Technical Research Institute, 6-50 Morinomiya 1-chome, Jyoto-ku , Osaka 536 , Japan.
H
H
Nakano
a Osaka Municipal Technical Research Institute, 6-50 Morinomiya 1-chome, Jyoto-ku , Osaka 536 , Japan.
S
S
Kitahata