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International Journal of Medicinal Mushrooms
Импакт фактор: 1.423 5-летний Импакт фактор: 1.525 SJR: 0.431 SNIP: 0.661 CiteScore™: 1.38

ISSN Печать: 1521-9437
ISSN Онлайн: 1940-4344

Выпуски:
Том 21, 2019 Том 20, 2018 Том 19, 2017 Том 18, 2016 Том 17, 2015 Том 16, 2014 Том 15, 2013 Том 14, 2012 Том 13, 2011 Том 12, 2010 Том 11, 2009 Том 10, 2008 Том 9, 2007 Том 8, 2006 Том 7, 2005 Том 6, 2004 Том 5, 2003 Том 4, 2002 Том 3, 2001 Том 2, 2000 Том 1, 1999

International Journal of Medicinal Mushrooms

DOI: 10.1615/IntJMedMushr.v13.i1.90
pages 73-82

Partial Purification and Characterization of Polyphenoloxidase from Culinary-Medicinal Royal Sun Mushroom (the Himematsutake), Agaricus brasiliensis S. Wasser et al. (Agaricomycetideae)

Akiko Matsumoto-Akanuma
School of Pharmacy, Department of Molecular Biology, Tokyo University of Pharmacy and Life Science, 1432-1 Horinouchi, Hachioji, Tokyo 192-0392, Japan
Satoshi Akanuma
Department of Molecular Biology, Tokyo University of Pharmacy and Life Sciences, Hachioji, Tokyo, Japan
Masuro Motoi
Toei Pharmaceutical Co. Ltd., 2-5-3 Iguchi, Mitaka, Tokyo 181-0011; Laboratory for Immunopharmacology of Microbial Products, School of Pharmacy, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo 192-0392, Japan
Akihiko Yamagishi
Department of Molecular Biology, Tokyo University of Pharmacy and Life Science, 1432-1 Horinouchi, Hachioji, Tokyo 192-0392, Japan
Naohito Ohno
Laboratory for Immunopharmacology of Microbial Products, Tokyo University of Pharmacy and Life Science, Tokyo, Japan

Краткое описание

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.


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