RT Journal Article
ID 1621bd541b5bf753
A1 Matsumoto-Akanuma, Akiko
A1 Akanuma, Satoshi
A1 Motoi, Masuro
A1 Yamagishi, Akihiko
A1 Ohno, Naohito
T1 Partial Purification and Characterization of Polyphenoloxidase from Culinary-Medicinal Royal Sun Mushroom (the Himematsutake), Agaricus brasiliensis S. Wasser et al. (Agaricomycetideae)
JF International Journal of Medicinal Mushrooms
JO IJM
YR 2011
FD 2011-03-22
VO 13
IS 1
SP 73
OP 82
K1 medicinal mushrooms
K1 Royal Sun mushroom
K1 Agaricus brasiliensis
K1 Triton X-114
K1 polyphenoloxidase
K1 tyrosinase
K1 SDS activation
AB The Royal Sun mushroom, the Himematsutake culinary-medicinal mushroom, Agaricus brasiliensis has several polyphenoloxidase activities in a broad sense. Here we report the partial purification of tyrosinase-type polyphenoloxidase (PPO). PPO is purified from A. brasiliensis without browning using a two-phase partitioning with Triton X-114 and ammonium sulfate fractionation. Partially denaturing SDS-PAGE (sodium dodecyl sulfate-polyacrylamide electrophoresis) staining with L-3,4-dihydroxyphenylalanine was performed and the indicated molecular sizes were approximately 70 kDa and 45 kDa. The purified enzyme is in its latent state and can be activated maximally in the presence of 1.6 mM sodium dodecyl sulfate (SDS). This enzyme catalyzes two distinct reactions, monophenolase and diphenolase activity, and the monophenolase activity showed a lag time typical of polyphenoloxidase. The Km value for 4-tert-butylcatechol was quite similar in the presence and absence of SDS, but the apparent Vmax value was increased 2.0-fold by SDS. Mimosine was a typical competitive inhibitor with Ki values of 138.2 μM and 281.0 μM n the presence and absence of SDS, respectively.
PB Begell House
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