Yukiguni Maitake Co.

Minamiuonuma, Japan

Yukiguni Maitake Co.

Minamiuonuma, Japan
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Masuda Y.,Kobe Pharmaceutical University | Nakayama Y.,Kobe Pharmaceutical University | Tanaka A.,Yukiguni Maitake Co. | Naito K.,Yukiguni Maitake Co. | Konishi M.,Kobe Pharmaceutical University
PLoS ONE | Year: 2017

Maitake α-glucan, YM-2A, isolated from Grifola frondosa, has been characterized as a highly α-1,6-branched α-1,4 glucan. YM-2A has been shown to possess an anti-virus effect in mice; however, it does not directly inhibit growth of the virus in vitro, indicating that the anti-virus effect of YM-2A might be associated with modulation of the host immune system. In this study, we found that oral administration of YM-2A could inhibit tumor growth and improve survival rate in two distinct mouse models of colon-26 carcinoma and B16 melanoma. Orally administered YM-2A enhanced antitumor immune response by increasing INF-γ-expressing CD4+ and CD8+ cells in the spleen and INF-γ-expressing CD8+ cells in tumor-draining lymph nodes. In vitro study showed that YM-2A directly activated splenic CD11b+ myeloid cells, peritoneal macrophages and bone marrow-derived dendritic cells, but did not affect splenic CD11b-lymphocytes or colon-26 tumor cells. YM-2A is more slowly digested by pancreatic α-Amylase than are amylopectin and rabbit liver glycogen, and orally administered YM-2A enhanced the expression of MHC class II and CD86 on dendritic cells and the expression of MHC class II on macrophages in Peyer's patches. Furthermore, in vitro stimulation of YM-2A increased the expression of pro-inflammatory cytokines in Peyer's patch CD11c+ cells. These results suggest that orally administered YM-2A can activate dendritic cells and macrophages in Peyer's patches, inducing systemic antitumor T-cell response. Thus, YM-2A might be a candidate for an oral therapeutic agent in cancer immunotherapy. © 2017 Masuda et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.


PubMed | Slovenian National Institute of Chemistry, University of Queensland, Daiichi Sankyo, French Institute of Health and Medical Research and 6 more.
Type: | Journal: FASEB journal : official publication of the Federation of American Societies for Experimental Biology | Year: 2016

We identified a novel, nontoxic mushroom protein that specifically binds to a complex of sphingomyelin (SM), a major sphingolipid in mammalian cells, and cholesterol (Chol). The purified protein, termed nakanori, labeled cell surface domains in an SM- and Chol-dependent manner and decorated specific lipid domains that colocalized with inner leaflet small GTPase H-Ras, but not K-Ras. The use of nakanori as a lipid-domain-specific probe revealed altered distribution and dynamics of SM/Chol on the cell surface of Niemann-Pick type C fibroblasts, possibly explaining some of the disease phenotype. In addition, that nakanori treatment of epithelial cells after influenza virus infection potently inhibited virus release demonstrates the therapeutic value of targeting specific lipid domains for anti-viral treatment.-Makino, A., Abe, M., Ishitsuka, R., Murate, M., Kishimoto, T., Sakai, S., Hullin-Matsuda, F., Shimada, Y., Inaba, T., Miyatake, H., Tanaka, H., Kurahashi, A., Pack, C.-G., Kasai, R. S., Kubo, S., Schieber, N. L., Dohmae, N., Tochio, N., Hagiwara, K., Sasaki, Y., Aida, Y., Fujimori, F., Kigawa, T., Nishibori, K., Parton, R. G., Kusumi, A., Sako, Y., Anderluh G., Yamashita, M., Kobayashi, Te., Greimel, P., Kobayashi, To. A novel sphingomyelin/cholesterol domain-specific probe reveals the dynamics of the membrane domains during virus release and in Niemann-Pick type C.


Shimoda T.,Yukiguni Maitake Co. | Shimoda T.,Chiba University | Shirouchi T.,Yukiguni Maitake Co. | Suzuki A.,Chiba University | And 2 more authors.
Journal of Wood Science | Year: 2012

The storage of spent maitake culture medium (SMCM) under various conditions was investigated as a potential pretreatment of SMCM for increased ethanol conversion. When SMCM was stored at 25°C for 12 weeks, the glucose yield by enzymatic saccharification increased from 22 to 52%. Selective degradation of lignin and hemicellulose occurred in SMCM during storage. The optimal storage temperature of SMCM was at the active growing temperature of maitake mycelium, which is between 25 and 30°C. Storage of SMCM under anaerobic conditions did not increase the glucose yield compared to non-stored conditions. The glucose yield from the SMCM stored for 4 weeks at 25°C was increased by about 30% with either NaOH or vibrating ball milling pretreatment. After 12 weeks of storage, the glucose yield from SMCM without any other pretreatment was higher than that of non-stored SMCM with additional pretreatments. An ethanol yield of 42. 1% was obtained from SMCM stored for 12 weeks by simultaneous saccharification and fermentation, which was comparable to yields after NaOH (41. 3%) or vibrating ball milling (44. 1%) pretreatments. Therefore, storage of SMCM is a very useful pretreatment for bioethanol production. © 2012 The Japan Wood Research Society.


Saeki N.,Kinki University | Takeda H.,Kinki University | Takeda H.,Yukiguni Maitake Co. | Tanesaka E.,Kinki University | Yoshida M.,Kinki University
Mycoscience | Year: 2011

The white-rot basidomycete Lentinula edodes often produces the lignin-degrading enzymes manganese peroxidase (MnP; EC 1.11.1.13) and laccase (Lcc; EC 1.10.3.2) in sawdust-based media. In the present study, MnP from L. edodes was induced under liquid culture supplemented with sawdust extracts of Castanopsiscuspidata. Lcc activity was induced by the addition of 2 mM CuSO 4·5H 2O into the same media 7 days after initial inoculation. Phenoloxidase enzymes were distinguished by polyacrylamide gel electrophoresis (native-PAGE), followed by sequential enzymatic staining with an improved staining solution. The isozyme bands detected under MnP-induced conditions were identified as manganese peroxidase (lemnp2) and bands detected under Lcc-induced conditions were identified as laccase (lcc1) by Q-TOF mass spectrometry. © 2010 The Author(s).


Bhat H.B.,Saitama University | Bhat H.B.,RIKEN | Kishimoto T.,RIKEN | Abe M.,RIKEN | And 13 more authors.
Journal of Lipid Research | Year: 2013

A mixture of sphingomyelin (SM) and cholesterol (Chol) exhibits a characteristic lipid raft domain of the cell membranes that provides a platform to which various signal molecules as well as virus and bacterial proteins are recruited. Several proteins capable of specifically binding either SM or Chol have been reported. However, proteins that selectively bind to SM/Chol mixtures are less well characterized. In our screening for proteins specifically binding to SM/Chol liposomes, we identified a novel ortholog of Pleurotus ostreatus, pleurotolysin (Ply)A, from the extract of edible mushroom Pleurotus eryngii, named PlyA2. Enhanced green fluorescent protein (EGFP)-conjugated PlyA2 bound to SM/Chol but not to phosphatidylcholine/Chol liposomes. Cell surface labeling of PlyA2-EGFP was abolished after sphingomyelinase as well as methyl-β- cyclodextrin treatment, removing SM and Chol, respectively, indicating that PlyA2-EGFP specifically binds cell surface SM/Chol rafts. Tryptophan to alanine point mutation of PlyA2 revealed the importance of C-terminal tryptophan residues for SM/Chol binding. Our results indicate that PlyA2- EGFP is a novel protein probe to label SM/Chol lipid domains both in cell and model membranes. Copyright © 2013 by the American Society for Biochemistry and Molecular Biology, Inc.


Patent
Yukiguni Maitake Co. | Date: 2011-02-04

A method for treating a lignocellulose raw material so as to facilitate a pulverization treatment that is necessary for the efficient and effective use of a lignocellulose raw material as a raw material or resource for material conversion. When converting a lignocellulose raw material into sugar or a useful material, such as ethanol, with the aid of an enzyme or producing a biodegradable material derived from a lignocellulose raw material via a mechanical or chemical treatment, a lignocellulose raw material is treated with an enzyme prior to or simultaneously with the pulverization process, so that the viscosity of slurry comprising a lignocellulose raw material and water is lowered and the pulverization efficiency is improved.


Patent
Ming East West LLC and Yukiguni Maitake Co. | Date: 2010-07-30

A method of producing a beverage including: combining roasted, ground maitake mushroom with roasted, ground coffee beans to provide a maitake-coffee mixture, and brewing the maitake-coffee mixture; and a maitake-coffee beverage produced thereby.


It is an objective of the present invention to develop a Grifola-derived substance having advanced immunopotentiating activity and antitumor activity, which has a molecular weight lower than that of a conventionally known glucan-protein complex and is structurally different from such complex. A Grifola-derived low-molecular-weight substance is produced by the following steps 1) to 4):1) a step of thermally extracting mycelia or fruit bodies of Grifola with water;2) a step of adding alcohol to the obtained water-soluble extract fraction to a final concentration between 10% and 80% by volume, allowing the resulting solution to stand at a temperature between 1C and 40C, and removing matter floating on or in the solution or adhering to the wall surface of a vessel and a precipitate formed therein;3) a step of removing alcohol from the water-soluble fraction containing alcohol obtained in step 2) and collecting an adsorbed fraction from the obtained water-soluble fraction by anion-exchange column chromatography;4) a step of collecting a fraction with a molecular weight of 5000 or less by subjecting the adsorbed fraction to molecular sieving.


Patent
Riken, Yukiguni Maitake Co. and Ochanomizu University | Date: 2011-05-13

A protein being the following (A), (B), or (C): (A) a protein represented by the amino acid sequence of SEQ ID NO: 1; (B) a protein represented by an amino acid sequence in which one or a plurality of amino acid is substituted, deleted, inserted or added in the amino acid sequence of SEQ ID NO: 1, the protein having binding activity specific for a mixture of a sphingolipid and cholesterol; or (C) a protein represented by an amino acid sequence being at least 70% identical to the amino acid sequence of SEQ ID NO: 1.


Trademark
Yukiguni Maitake Co. | Date: 2011-10-26

Mushroom-based or mushroom extract-based dietetic foods adapted for medical use; other dietetic foods adapted for medical use; dietetic beverages adapted for medical use; baby foods; dietary food supplements. Dried mushrooms; processed mushrooms; mushroom-based or mushroom extract-based foods in the form of liquids, syrups (except for soft drinks and beverages), suspensions, emulsions, tablets, pills, powders, granules, capsules, candies, creams, pastes, sticks, chocolates, gums or gels; mushroom-containing or mushroom extract-containing processed vegetables or fruits; mushroom-containing or mushroom extract-containing protein for human consumption; mushroom-containing or mushroom extract-containing vegetable juices for cooking.

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