 | 福田 泰久 （フクタ ヤスヒサ）
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Last Updated :2024/04/25
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主に微生物（きのこ、カビ、酵母、細菌）由来の酵素を用いて、有用な物質の合成に応用させることを目的に研究を行っております。特に最近では食品微生物に関して重点的に実験をしております。
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- 応用微生物学 酵素化学工学
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- 主に微生物（きのこ、カビ、酵母、細菌）由来の酵素を用いて、有用な物質の合成に応用させることを目的に研究を行っております。特に最近では食品微生物に関して重点的に実験をしております。
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論文
- Atsushi Kurata; Shimpei Takeuchi; Ryo Fujiwara; Kento Tamura; Tomoya Imai; Shino Yamasaki-Yashiki; Hiroki Onuma; Yasuhisa Fukuta; Norifumi Shirasaka; Koichi UegakiBioscience, biotechnology, and biochemistry 2023年05月We characterized the membrane vesicle fraction (RD MV fraction) from bacterial strain RD055328, which is related to members of the genus Companilactobacillus and Lactiplantibacillus plantarum. RD MVs and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were detected in the RD MV fraction. Immunoglobulin A (IgA) was produced by Peyer's patches cells following the addition of the RD MV fraction. In the presence of the RD MV fraction, RAW264 cells produced the pro-inflammatory cytokine IL-6. Recombinant GAPDH probably induced the production of IL-6 by RAW264 cells via superficial Toll-like receptor 2 (TLR2) recognition. A confocal laser scanning microscopy image analysis indicated that RD MVs and GAPDH were taken up by RAW264 cells. GAPDH wrapped around RAW264 cells. We suggest that GAPDH from strain RD055328 enhanced the production of IgA by acquired immune cells via the production of IL-6 by innate immune cells through TLR2 signal transduction.
- Collibacillus ludicampi gen. nov., sp. nov., a new soil bacterium of the family Alicyclobacillaceae.Toru Jojima; Yuki Ioku; Yasuhisa Fukuta; Norifumi Shirasaka; Yoshinobu Matsumura; Miho MoriInternational journal of systematic and evolutionary microbiology 73 5 2023年05月
- GPDプロモーターによるハイグロマイシンB耐性トキイロヒラタケ単核体の効率的形質転換福田泰久; 平山朋美; 北野修也; 佐藤魁; 魚川岳人; 白坂憲章日本きのこ学会誌 28 4 171 - 174 2020年12月 [査読有り]
- トキイロヒラタケNBRC31859株由来子実体形成および非形成単胞子分離株の取得Yasuhisa Fukuta; Tomomi Hirayama; Norifumi Shirasaka日本きのこ学会誌 28 3 117 - 122 2020年08月
- Onuma H; Hara K; Sugita K; Kano A; Fukuta Y; Shirasaka NJournal of bioscience and bioengineering 128 6 669 - 676 2019年12月 [査読有り]
- Teruyoshi Tanaka; Hiroki Onuma; Takashi Shigihara; Eiichi Kimura; Yasuhisa Fukuta; Norifumi Shirasaka; Tatsuya Moriyama; Yoshimi HommaJournal of bioscience and bioengineering 128 5 622 - 629 2019年11月 [査読有り]
In recent years, the number of patients with osteoporosis has increased as population grows older. Therefore, the chemoprevention of osteoporosis by better nutrition is important. White-rot fungi degrades milled wood lignin for growth and development. This degradation results in the formation of phenolic compounds such as syringic acid (SA) and vanillic acid (VA). In the artificial culture of edible mushrooms using a mushroom bed, the disposal of waste beds after mushroom cultivation is an important issue. The present study investigated the presence and amount of both SA and VA in the discarded waste beds after mushroom cultivation. The extracts from waste beds after cultivation of shiitake mushrooms, Lentinula edodes; buna shimeji, Hypsizygus marmoreus; maitake, Grifola frondosa; king trumpet mushrooms, Pleurotus eryngii; and butterscotch mushrooms, Pholiota microspora were analyzed using high performance liquid chromatography. Although the content of SA and VA was considerably different among the mushrooms, SA and VA were present in extracts obtained from all the waste beds. We also demonstrated that SA and VA exert their anti-osteoporotic effect independently of the estrogen receptor-mediated pathway using murine monocytic RAW264.7 cells, ovariectomized mice, and human breast cancer MCF-7 cells. Thus, these results suggest that the extracts are effective sources of SA and VA, which are effective in preventing osteoporosis. - Fukuta Y; Kamei K; Matsui A; Fuji Y; Onuma H; Shirasaka NBioscience, biotechnology, and biochemistry 83 7 1354 - 1361 2019年07月 [査読有り]
- 消費者の食用きのこに対する価値認識と人工栽培マツタケへの潜在的需要 －アンケート調査を用いたセグメンテーションによる分析ー大石卓史; 福田泰久; 白坂憲章日本きのこ学会誌 27 1 13 - 20 2019年04月 [査読有り]
- 固体培地培養におけるマツタケ菌糸体バイオマス定量法の開発大沼広宜; 原 健人; 張正煕; 白坂憲章; 福田泰久日本きのこ学会誌 26 4 156 - 163 2019年01月 [査読有り]
- Enzymatic characterization of an extracellular glucoamylase from Tricholoma matsutake and its cloning and secretory expression in Pichia pastorisOnuma H; Uchiyama H; Hara K; Fukuta Y; Shirasaka NBiosci Biotechnol Biochem. 82 2180 - 2190 2018年12月 [査読有り]
- Tanaka T; Kawaguchi N; Zaima N; Moriyama T; Fukuta Y; Shirasaka NJournal of Natural Medicines 71 4 632 - 641 Springer Japan Production Department 2017年10月 [査読有り]
- Kurata A; Fukuta Y; Mori M; Kishimoto N; Shirasaka NGenome announcements 4 3 2016年06月 [査読有り]
- Sakdapetsiri Chatsuda; 白坂 憲章; 福田泰久J Basic Microbiol 56 5 469 - 479 2016年05月 [査読有り]
A total of 123 actinomycetes was isolated from 12 varieties of wild orchids and screened for potential antagonistic activity against Phytophthora, which causes black rot disease in orchids. In vitro and in vivo experimental results revealed that Streptomyces sp. strain 9X166 showed the highest antagonistic activity; its -1,3-glucanase production ability was a key mechanism for growth inhibition of the pathogen. PCR amplification and DNA sequencing of the 16S ribosomal RNA gene allowed the identification of this strain, with high similarity (99.93%) to the novel species Streptomyces similaensis. The glucanase enzyme, purified to homogeneity by anion exchange and gel filtration chromatography, showed a specific activity of 58Umg(-1) (a 3.9-fold increase) and yield of 6.4%. The molecular weight, as determined by SDS-PAGE and gel filtration, was approximately 99 and 80kDa, respectively, suggesting that the enzyme was a monomer. The purified enzyme showed the highest substrate specificity to laminarin, indicating that it was -1,3-glucanase. The hydrolyzed products of cello-oligosaccharides suggested that this enzyme was endo-type -1,3-glucanase. Streptomyces sp. 9X166 culture filtrate, possessing -1,3-glucanase activity, could degrade both freeze-dried and living mycelium. This is the first report on a -1,3-glucanase-producing Streptomyces sp. that could be an effective biocontrol agent for black rot disease in orchids. - Daisuke Matsui; Do-Hyun Im; Asami Sugawara; Yasuhisa Fukuta; Shinya Fushinobu; Kimiyasu Isobe; Yasuhisa AsanoFEBS OPEN BIO 4 220 - 228 2014年 [査読有り]
In this study, it was shown for the first time that L-amino acid oxidase of Pseudomonas sp. AIU813, renamed as L-amino acid oxidase/monooxygenase (L-AAO/MOG), exhibits L-lysine 2-monooxygenase as well as oxidase activity. L-Lysine oxidase activity of L-AAO/MOG was increased in a p-chloromercuribenzoate (p-CMB) concentration-dependent manner to a final level that was fivefold higher than that of the non-treated enzyme. In order to explain the effects of modification by the sulfhydryl reagent, saturation mutagenesis studies were carried out on five cysteine residues, and we succeeded in identifying L-AAO/MOG C254I mutant enzyme, which showed five-times higher specific activity of oxidase activity than that of wild type. The monooxygenase activity shown by the C254I variant was decreased significantly. Moreover, we also determined a high-resolution three-dimensional structure of L-AAO/MOG to provide a structural basis for its biochemical characteristics. The key residue for the activity conversion of L-AAO/MOG, Cys-254, is located near the aromatic cage (Trp-418, Phe-473, and Trp-516). Although the location of Cys-254 indicates that it is not directly involved in the substrate binding, the chemical modification by p-CMB or C254I mutation would have a significant impact on the substrate binding via the side chain of Trp-516. It is suggested that a slight difference of the binding position of a substrate can dictate the activity of this type of enzyme as oxidase or monooxygenase. (C) 2014 The Authors. Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies. - Fukuta, Y; Ito, K; Shirasaka, N; Kusuda, M; Mihara, S; Yamanaka, K; Terashita, TMushroom Sci. Biotechnol. 21 4 172 - 176 日本きのこ学会 2014年 [査読有り]
ブナシメジ(Hypsizygus marmoreus)栽培において,菌かき後に培養基内で活性が上昇する中性プロテアーゼは,本菌の子実体形成に深く関わることが考えられる.子実体収穫後の培養基をプロテアーゼ源として,菌糸体内由来の中性プロテアーゼ(PE-4)の酵素精製と諸性質の検討を行った.PE-4は,セリンプロテアーゼ阻害剤であるPMSF,AprotininとPefabloc[○!R]SCによって完全に活性を失ったが,Phosphoramidonに感受性を示さなかった.阻害剤の影響およびN末端アミノ酸配列の結果から,PE-4はセリンプロテアーゼであると結論した.金属プロテアーゼ阻害剤であるPhosphoramidonは,本菌の子実体形成を著しく阻害するため,PE-4は子実体形成に深く関わらないことが示唆された.菌かき後から子実体成熟期における菌糸体より粗酵素を抽出し,中性プロテアーゼ活性に対するPhosphoramidon,PMSFとEDTAの阻害度合を測定したところ,PMSFによる完全な阻害は受けなかった.子実体形成においては,PE-4以外に活性化されているプロテアーゼの重要性が示唆された. - Fukuta, Y; Shirasaka, N; Ikenaga, C; Kusuda, M; Yamauchi, M; Terashita, TMushroom Sci. Biotechnol. 21 3 123 - 128 日本きのこ学会 2013年 [査読有り]
シロキクラゲ(Tremella fuciformis)培養基から抽出した粗酵素は,セルロース粉末,Avicelとp-nitrophenyl-β-d-glucopyranosideに加水分解活性を示し,本菌のエキソ型セルラーゼとβ-グルコシダーゼの生産性が示唆された.しかしながら,エンド型セルラーゼの活性は認められなかった.「Companion fungus」と考えられるクロコブタケ(Hypoxylon truncatum)由来の粗酵素液は,上記基質に対する活性に加えてカルボキシメチルセルロース(CMC)にも活性を示し,エンド型セルラーゼの生産性が示唆された.CMCを基質として各種クロマトグラフィーを用いてH.truncatum由来セルラーゼの精製を行い,酵素化学的諸性質を解析した.SDS-PAGEとゲル濾過で確認された単一タンパクの分子量は,それぞれ46,000と41,000を示し、本酵素は単量体であった.4糖(cellotetraose)以上のオリゴ糖に加水分解活性を示し,2糖(cellobiose)まで生成可能であった.H.trucatumとの共培養条件下において,T.fuciformisのセルロース分解機構における微弱もしくは欠落したエンド型加水分解を,本酵素が補うことが示唆された. - Iwamoto, K; Yoshida, T; Kusuda, M; Fukuta, Y; Terashita, T; Shirasaka, NMushroom Sci. Biotechnol. 21 16 - 22 2013年 [査読有り]
- 白坂 憲章; 福田 泰久; 寺下 隆夫日本きのこ学会誌 20 3 141 - 146 日本きのこ学会 2012年11月
- Kimiyasu Isobe; Asami Sugawara; Hanako Domon; Yasuhisa Fukuta; Yasuhisa AsanoJOURNAL OF BIOSCIENCE AND BIOENGINEERING 114 3 257 - 261 2012年09月 [査読有り]
An L-amino acid oxidase was found from a newly isolated strain. Pseudomonas sp. AIU 813. This enzyme was remarkably induced by incubation with L-lysine as a nitrogen source, and efficiently purified using an affinity chromatography with L-lysine as ligand. The enzyme oxidized L-lysine, L-ornithine and L-arginine, but not other L-amino acids and D-amino acids. The oxidase activity for L-lysine was detected in a wide pH range, and its optimal was pH 7.0. In contrast, the oxidase activity for L-ornithine and L-arginine was not shown in acidic region from pH 6.5, and optimal pH for both substrates was 9.0. The enzyme was a Flavoprotein and composed of two identical subunits with molecular mass of 54.5 kDa. The N-terminal amino acid sequence was similar to that of putative Flavin-containing amine oxidase and putative tryptophan 2-monooxygenase, but not to that of L-amino acid oxidases. (C) 2012, The Society for Biotechnology, Japan. All rights reserved. - Norifumi Shirasaka; Masao Naitou; Kazuki Okamura; Mizuho Kusuda; Yasuhisa Fukuta; Takao TerashitaMYCOSCIENCE 53 5 354 - 364 2012年09月 [査読有り]
An enzyme from Aspergillus oryzae KSK-3, isolated from commercial rice-koji for miso brewing, showed fibrinolytic activity in liquefied rice culture and was analyzed. A culture filtrate of A. oryzae KSK-3 was concentrated by ultrafiltration and subsequently purified to electrophoretic homogeneity by ammonium sulfate precipitation, ion-exchange chromatography, and gel filtration. The molecular weight of the purified enzyme was estimated to be approximately 30 kDa by SDS-PAGE and high-performance liquid chromatography-size exclusion chromatography. Its maximum fibrinolytic activity was observed at pH 6 and 50A degrees C. The purified protease was stable between pH 4 and 9, at temperatures of up to 50A degrees C. The activity of the enzyme was highest with S-2238 and was considerably inhibited by phenylmethylsufonyl fluoride and pefabloc SC. These results indicate that the enzyme is a serine protease. Moreover, the enzyme is edible and exhibited very high productivity (2,960 U urokinase per milliliter of culture broth). Taken together, the findings of this study indicate that the A. oryzae KSK-3 enzyme may be used as a natural agent for oral fibrinolytic therapy and nutraceutical applications. - Shirasaka, N; Yamaguchi, Y; Yoshioka, S; Fukuta, Y; Terashita, TMushroom Sci. Biotechnol. 20 147 - 153 2012年 [査読有り]
- Mohammad Dadashipour; Yasuhisa Fukuta; Yasuhisa AsanoPROTEIN EXPRESSION AND PURIFICATION 77 1 92 - 97 2011年05月 [査読有り]
Low protein solubility and inclusion body formation represent big challenges in production of recombinant proteins in Escherichia coli. We have recently reported functional expression of hydroxynitrile lyase from Manihot esculenta, MeHNL, in E. coli with high in vivo solubility and activity using directed evolution. As a part of attempts to clarify the mechanism of this phenomenon, we have described the possibility of expression of the highly active and soluble mutant MeHNL-His103Leu as well as wild-type enzyme in several expression systems. Methylotrophic yeast Pichia pastoris, protozoan host Leishmania tarentolae and two cell-free translations, including an E. coli lysate (WakoPURE system) and wheat germ translation system were used to compare expression profiles of the genes. Two distinguishable protein expression patterns were observed in prokaryotic and eukaryotic-based systems. The wild-type and mutant enzyme showed high activity for both genes (up to 10 U/ml) in eukaryotic hosts P. pastoris and L tarentolae, while those of E. coli exhibited about 1 and 15 U/ml, respectively. The different activity level in prokaryotic systems but the same level among the eukaryotic hosts indicate the phenomenon is specific to the E. coli system. Both the wild-type and mutant enzymes were functionally expressed in eukaryotic systems, probably using the folding assistants such as chaperones. Properties of expression systems used in this study were precisely compared, too. (c) 2011 Elsevier Inc. All rights reserved. - Yasuhisa Fukuta; Samik Nanda; Yasuo Kato; Hiroya Yurimoto; Yasuyoshi Sakai; Hidenobu Komeda; Yasuhisa AsanoBIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY 75 2 214 - 220 2011年02月 [査読有り]
PmHNL, a hydroxynitrile lyase from Japanese apricot ume (Prunus mume) seed was purified to homogeneity by ammonium sulfate fractionation and chromatographic steps. The purified enzyme was a monomer with molecular mass of 58 kDa. It was a flavoprotein similar to other hydroxynitrile lyases of the Rosaceae family. It was active over a broad temperature, and pH range. The N-terminal amino acid sequence (20 amino acids) was identical with that of the enzyme from almond (Prunus dulcis). Based on the N-terminal sequence of the purified enzyme and the conserved amino acid sequences of the enzymes from Pr. dulcis, inverse PCR method was used for cloning of a putative PmHNL (PmHNL2) gene from a Pr. mume seedling. Then the cDNA for the enzyme was cloned. The deduced amino acid sequence was found to be highly similar (95%) to that of an enzyme from Pr. serotina, isozyme 2. The recombinant Pichia pastoris transformed with the PmHNL2 gene secreted an active enzyme in glycosylated form. - Fukuta, Y; Koizumi, S; Komeda, H; Asano, YEnzyme Microb. Technol. 46 3-4 237 - 245 2010年03月 [査読有り]
Rhodococcus sp. strain Oct1 utilizing omega-octalactam as a sole source of carbon and nitrogen was isolated from soil. omega-Octalactam hydrolyzing enzyme was purified to homogeneity. The purified enzyme has a molecular weight of approximately 48,100 by SDS polyacrylamide gel electrophoresis and 99,1100 by gel filtration, indicating that the enzyme consists of 2 subunits. The purified enzyme catalyzed the hydrolysis of omega-octalactam to form 8-aminooctanoic acid at a rate of 3.95 U/mg. The purified enzyme also acted on omega-heptalactam, omega-laurolactam, nitroacetoanilide substitutions, and various aliphatic amides. The most suitable substrate was o-nitroacetanilide for the enzyme (11.6 U/mg). The enzyme belongs to aryl acylamidase. The gene for the enzyme was cloned and the deduced amino acid sequence showed similarity to omega-laurolactam hydrolase from Rhodococcus sp. U224 (51%) and putative aryl acylamidase from Nocardia farcinica IFM 10152 (98%), and N-terminal amino acid sequence (28 residues) of aryl acylamidase from Nocardia globerula IFO 13510 (92%). Aryl acylamidases and 6-aminohexanoate-cyclic-dimer hydrolases are in the same phylogenic lineage. These enzymes were mostly active toward non-natural amides. From phylogenic analysis, these enzymes were classified into amidase signature family. The enzyme was produced in a soluble form as a fusion protein (extension of 13 amino acids at C-terminal) in Escherichia coli. (C) 2009 Elsevier Inc. All rights reserved. - Fukuta, Y; Komeda, H; Yoshida, Y; Asano, YBiosci. Biotechnol. Biochem. 73 5 980 - 986 2009年05月 [査読有り]
The genes encoding omega-laurolactam hydrolases from Cupriavidus sp. T7, Acidovorax sp. T31, Cupriavidus sp. U124, and Sphingomonas sp. U238 were cloned and sequenced. Nucleotide and amino acid sequence analysis of the four genes indicated that the primary structures of these omega-laurolactam hydrolases are significantly similar to the 6-aminohexanoate-cyclic-dimer hydrolase (EC 3.5.2.12). These genes were expressed in Escherichia coli.. and the omega-laurolactam hydrolysing activity of the recombinant enzymes was compared with that of 6-aminohexanoate-cyclic-dimer hydrolase from Arthrobacter sp. K172. The enzyme from Acidovorax sp. T31 was most successfully expressed in E. coli. Cell-free extract of the recombinant strain was used for the synthesis of 12-aminolauric acid from omega-laurolactam by "enzymatic transcrystallization," because crystalline omega-laurolactam added into the enzyme solution was converted to crystalline 12-aminolauric acid (>= 97.3% yield). Under the optimum conditions, 208 g/l of 12-aminolauric acid was produced in 17 h. The resulting pure product was identical to authentic 12-aminolauric acid. - Asano, Y; Fukuta, Y; Yoshida, Y; Komeda, HBiosci. Biotechnol. Biochem. 72 8 2141 - 2150 2008年08月 [査読有り]
Several omega-laurolactam degrading microorganisms were isolated from soil samples. These strains were capable of growing in a medium containing omega-laurolactam as sole source of carbon and nitrogen. Among them, five strains (T7, T31, U124, U224, and U238) were identified as, Cupriavidus sp. T7, Acidovorax sp. T31, Cupriavidus sp. U124, Rhodococcus sp. U224, and Sphingomonas sp. U238, respectively. The w-laurolactam hydrolyzing enzyme from Rhodococcus sp. U224 was purified to homogeneity, and its enzymatic properties were characterized. The enzyme acts on omega-octalactam and omega-laurolactam, but other lactam compounds, amides and amino acid amides, cannot be substrates. The enzyme, gene was cloned, and the deduced amino acid sequence showed high homology with 6-aminohexanoate-cyclic-dimer hydrolase (EC 3.5.2.12) from Arthrobacter sp. K172 and Pseudomonas sp. NK87. Enzymatic synthesis of 12-aminolauric acid was performed using partially purified w-laurolactam hydrolase from Rhodococcus sp. U224.
MISC
- 大石卓史; 大石卓史; 財満信宏; 財満信宏; 福田泰久; 白坂憲章 日本きのこ学会誌 28 (4) 2021年
- 湯村直樹; 中沢威人; 大沼広宜; 泉津弘佑; 入江俊一; 福田泰久; 白坂憲章; 坂本正弘; 本田与一 リグニン討論会講演集 62nd 56‐59 2017年10月
- 岩本 和子; 吉田 敬洋; 福田 泰久; 寺下 隆夫; 白坂 憲章 日本生物工学会大会講演要旨集 64 35 -35 2012年
- 松井大亮; 福田泰久; 礒部公安; 浅野泰久 酵素工学研究会講演会講演要旨集 68th 63 2012年
- 福田 泰久; 米田 英伸; 吉田 洋一; 浅野 泰久 日本生物工学会大会講演要旨集 20 163 -163 2008年
- 福田 泰久; 米田 英伸; 吉田 洋一; 浅野 泰久 日本生物工学会大会講演要旨集 18 92 -92 2006年
- 福田 泰久; 米田 英伸; 吉田 洋一; 浅野 泰久 日本生物工学会大会講演要旨集 17 110 -110 2005年
受賞
共同研究・競争的資金等の研究課題
- 日本学術振興会：科学研究費助成事業研究期間 : 2019年04月 -2022年03月代表者 : 福田 泰久マツタケの形質転換法確立を目指し、ホスト株となる単核体の取得と、プロトプラスト‐PEG法によるマツタケ遺伝子組換え技術の開発を目的に研究を行った。しかしながら、プロトプラストを研究期間中に再生させることはできなかった。現在は、自然界より分離したマツタケ細胞壁成分分解微生物由来のα-1,3-グルカナーゼを利用してさらに大量にプロトプラストを調整し、再生実験を継続して行っている。一方、同じ担子菌類を用いた遺伝子組換え実験として、子実体形成が可能なトキイロヒラタケをモデル実験に用いた。本実験で確立した方法により、ピンク色素タンパク遺伝子（PsPCP）の発現を抑制させ、白色子実体が形成された。
- 日本学術振興会：科学研究費助成事業研究期間 : 2014年04月 -2017年03月代表者 : 白坂 憲章; 福田 泰久食用きのこのγ-アミノ酪酸（GABA）生成系を明らかにするために、機能性成分であるGABAの生成に関与する酵素をマイタケ、シイタケ、エノキタケから精製し、その性質を検討した。その結果マイタケ、エノキタケの酵素はグルタミン酸とのみ反応しグルタミン酸脱炭酸酵素（GAD）と推定されたが、シイタケの酵素はグルタミン酸以外にもアスパラギン酸も基質とすることがわかった。シイタケの酵素については内部アミノ酸配列の情報からシイタケのゲノム上でフォスファチジルセリン脱炭酸酵素（PSD）と予測されている遺伝子がコードする酵素であると推定されたが、フォスファチジルセリンの脱炭酸反応を確認することはできなかった。
- 日本学術振興会：科学研究費助成事業研究期間 : 2014年04月 -2016年03月代表者 : 福田 泰久きのこの子実体形成には、各種プロテアーゼ群の活性化と不活化が深くかかわり、形態変化の制御因子として働いていることを報告してきた。シイタケゲノムデータベースよりプロテアーゼ様遺伝子群16種を抽出し、それぞれの遺伝子発現量を培養菌糸期と子実体原基形成期で相対定量比較し、子実体原基形成期では、g10056、g584、g1220、g4055遺伝子の発現量が顕著に増加し、子実体形成因子に関わることが示唆された。また、ブナシメジの子実体形成に深く関わるホスホラミドン感受性メタロプロテアーゼのアミノ酸配列を決定し、Fungalysin(Peptidase M38 family)であることを解明した。