MISC - KANZAKI Hiroshi

Bioconversion of olive leaf constituents by Aspergillus solid state fermentation using an air flow type rotary solid state fermenter for laboratory use

辰巳七海, 橋本敦子, 奥川日菜乃, 三宅剛史, 伊藤一成, 谷野有佳, 竹内赴登, 山下秀行, 内田真美, 三木翔平, 吉田靖弘, 徐恵美, 菊地敬一, 深野夏暉, 仁戸田照彦, 仁戸田照彦, 神崎浩, 神崎浩

日本農芸化学会大会講演要旨集(Web)   2023   2023

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Bioconversion of skin and seed constituents by Aspergillus solid state fermentation of wine pomace

藤田彩楓, 奥川日菜乃, 橋本敦子, 三宅剛史, 伊藤一成, 谷野有佳, 山下秀行, 中川拓郎, 平野幸司, 仁戸田照彦, 仁戸田照彦, 神崎浩, 神崎浩

日本農芸化学会大会講演要旨集(Web)   2023   2023

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Creation of highly functionalized Japanese wine pomace koji using koji mold solid culture technology

神崎浩, 仁戸田照彦, 伊藤一成, 谷野有佳, 竹内赴登

Annual Report of the Okayama Foundation for Science and Technology   32 ( 32 )   26 - 30   2023

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Analysis of MS/MS fragmentation patterns for search of new asteltoxin analogs with a unique α-pyrone moiety

三谷尚大, 神崎浩, 仁戸田照彦

日本農薬学会大会講演要旨集   47th (CD-ROM)   2022

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バイオサーファクタント・サーファクチンの自己集合特性への対カチオン種の違いによる影響

柳澤恵広, 柳澤恵広, 平敏彰, 仁戸田照彦, 神崎浩

日本農芸化学会中四国支部講演会講演要旨集(Web)   62nd   2022

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Effect of hot water pretreatment on Aspergillus solid state fermentation of wine pomace

奥川日菜乃, 橋本敦子, 三宅剛史, 伊藤一成, 谷野有佳, 山下秀行, 中川拓郎, 平野幸司, 仁戸田照彦, 神崎浩

日本農芸化学会大会講演要旨集(Web)   2022   2022

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Cyclo(Leu-Phe)oxidaseの幅広い基質特異性の定量的評価-天然の電子受容体を用いた活性測定と人工の電子受容体を用いた活性測定の比較-

坂口幸士朗, 仁戸田照彦, 神崎浩

日本農芸化学会中四国支部講演会講演要旨集(Web)   61st   2022

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Effect of steaming on Aspergillus solid state fermentation of olive leaves

橋本敦子, 奥川日菜乃, 三宅剛史, 伊藤一成, 谷野有佳, 山下秀行, 内田真美, 三木翔平, 吉田靖弘, 徐恵美, 菊地敬一, 仁戸田照彦, 神崎浩

日本農芸化学会大会講演要旨集(Web)   2022   2022

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麹菌固体培養による日本ワインパミス成分の高機能化(第2報)

奥川日菜乃, 橋本敦子, 三宅剛史, 伊藤一成, 谷野有佳, 山下秀行, 中川拓郎, 平野幸司, 仁戸田照彦, 神崎浩

日本農芸化学会西日本支部大会およびシンポジウム講演要旨集   2021 (CD-ROM)   2021

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Quantitative evaluation of the substrate specificity of cyclo(Leu-Phe)oxidase toward various cyclodipeptides

坂口幸士朗, 小西健太, 仁戸田照彦, 神崎浩

生体触媒化学シンポジウム講演要旨集   22nd (CD-ROM)   2020

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地方発バイオイノベーションの進展と機能性食素材開発 岡山発,産学連携フードイノベーション

神崎浩

Food Style 21   21 ( 1 )   2017

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地方発バイオイノベーションの進展と機能性食素材開発 岡山発,産学連携フードイノベーション 2)

神崎浩

Food Style 21   21 ( 2 )   2017

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MS/MSフラグメンテーションプロファイルを指標としたTMG-chitotriomycin類縁体の探索と構造活性相関

神崎浩, 臼木博一, 臼木博一, 仁戸田照彦, 畑中唯史

日本農薬学会大会講演要旨集   36th   2011

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Conversion of secondary metabolites from olive leaves by Baker's yeasts and the antioxidative activity of the product

Erika Akihisa, Yoshihiro Harada, Kumi Kobayashi, Akiko Hirano, Teruhiko Nitoda, Hiroshi Kanzaki

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC   62 ( 1 )   123 - 123   2010.1

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生物種の由来が異なる酵素を見分ける阻害剤 新規な構造と活性をもつ放線菌由来β-N-アセチルグルコサミニダーゼ阻害剤

仁戸田 照彦, 臼木 博一, 神崎 浩

化学と生物   47 ( 3 )   158 - 160   2009

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Language：Japanese   Publisher：Japan Society for Bioscience, Biotechnology, and Agrochemistry  

DOI： 10.1271/kagakutoseibutsu.47.158

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Bioassays: inhibitors of insect chitin-degrading enzymes

Teruhiko Nitoda, Hiroshi Kanzaki

Isolation, Identification and Characterization of Allelochemicals/Natural Products   499 - 412   2009

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DOI： 10.1201/b10195-21

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岡山大産米１００％使用，日本酒「おお岡大」― 学産学消から学産地消を目指して ―

神崎浩

日本生物工学会誌   86 ( 5 )   250 - 251   2008

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Other Link： https://projects.repo.nii.ac.jp/?action=repository_uri&item_id=303143

Development of natural cosmetic materials-microbial conversion of olive antioxidative constituents

Fragrance journal   36 ( 2 )   63 - 66   2008

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Other Link： http://search.jamas.or.jp/link/ui/2008137568

Purification and characterization of cyclo (Leu-Phe) oxidase of Streptomyces albulus expressed in Escherichia coli

Machiko Nagao, Rie Hirata, Teruhiko Nitoda, Hiroshi Kanzaki

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC   48 ( 3-4 )   108 - 108   2007.9

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A novel β-N-acetylglucosaminidase inhibitor of fungal origin

NITODA Teruhiko, TOYOOKA Miho, USUKI Hirokazu, OKUDA Toru, KANZAKI Hiroshi

32   123 - 123   2007.3

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Microorganisms with homocysteine thiolactone hydrolase: Screening and stereospecificity - Abstracts

Shozo Honda, Teruhiko Nitoda, Hiroshi Kanzaki

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC   42 ( 3-4 )   126 - 127   2006.11

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Further proof for wide substrate specificity of cyclo(Leu-Phe) oxidase from an actinomycete: Enzymatic conversion of cyclic dipeptides containing non-aromatic amino acids - Abstracts

Rie Hirata, Teruhiko Nitoda, Hiroshi Kanzaki

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC   42 ( 3-4 )   127 - 128   2006.11

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Cloning and expression of cyclo(Leu-Phe) oxidase gene from an actinomycete Streptomyces albulus K023

Machiko Nagao, Atsushi Morimoto, Takashi Tamura, Tohru Dairi, Hiroshi Kanzaki

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC   42 ( 3-4 )   126 - 126   2006.11

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Inhibitory specificity of a novel β-N-acetylglucosaminidase inhibitor HU-1

USUKI Hirokazu, NITODA Teruhiko, KANZAKI Hiroshi

31   81 - 81   2006.3

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Structure elucidation of a novel β-N-acetylglucosaminidase inhibitor HU-1

USUKI Hirokazu, NITODA Teruhiko, YAMAJI Nahoko, IWASHITA Takashi, KOMURA Hajime, KANZAKI Hiroshi

31   82 - 82   2006.3

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抗がん活性化合物の酵素合成

神崎 浩

ケミカルエンジニアリング   50, 902-906   2005

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2D15-5 Synthesis of novel fluoro analogs of albonoursin by precursor-directed biosynthesis

KANZAKI Hiroshi, TAKEDA Chikahiro, FUKATANI Yoshimi, NITODA Teruhiko

17   135 - 135   2005

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2J13-4 Thionation of a cell cycle inhibitor dehydrophenylahistin

KANZAKI Hiroshi, IKEDA Banri, TAMURA Takashi, NITODA Teruhiko

16   237 - 237   2004

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デヒドロアミノ酸残基を含む生理活性環状ジペプチド類

神崎 浩

生物工学会誌   81, 396-399 ( 9 )   396 - 399   2003

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Other Link： http://dl.ndl.go.jp/info:ndljp/pid/10514564

Enzymatic synthesis of a cell cycle inhibitor dehydrophenylahistin

Kanzaki Hiroshi, Ikeda Banri, Morimoto Atsushi, Nitoda Teruhiko

15   60 - 60   2003

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Chemical information-guided enzymatic synthesis of bioactive compounds

KANZAKI Hiroshi

Nippon Nōgeikagaku Kaishi   76, 539-541 ( 6 )   539 - 541   2002

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DOI： 10.1271/nogeikagaku1924.76.539

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環状ジペプチド脱水素酵素で新規生理活性物質を作る

神崎 浩

バイオサイエンスとインダストリー   60, 26-29   2002

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649 Purification and characterization of dipeptidase from a cyclic dipeptide-assimilating bacterium

Kanzaki Hiroshi, Miyoshi Kazuyuki, Nitoda Teruhiko

14   107 - 107   2002

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1 Production of Bioactive Compounds by Biosynthetic Enzymes of Dehydro Cyclic Dipeptides

Kanzaki Hiroshi, Yanagisawa Satohiro, Akazawa Kazumi, Ikeda Banri, Morimoto Atsushi, Nitoda Teruhiko

( 43 )   1 - 5   2001.9

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Cyclic dipeptides (CDPs, diketopiperazines) and their derivatives are widely distributed in nature as secondary metabolites. Although some of dehydro-CDPs are known as cell cycle inhibitors, their effective syntheses have not been reported. We found that Streptomyces albulus KO23, an albonoursin-producing actinomycete, had a biosynthetic pathway from cyclo (Leu-Phe) to albonoursin, cyclo (ΔLeu-ΔPhe) by the fed-batch culture and the resting-cell experiments. And this enzyme activity was found to be effectively extracted in the cell-free extract of this actinomycete. This is the first report for the dehydrogenation of amino acid residues at α,β-positions in CDPs. Furthermore, this enzyme system enables us to synthesize several didehydro- and tetradehydro-CDPs from the corresponding CDPs. Among dehydro-CDPs prepared, the tetradehydro-CDPs exhibited cytotoxicity, while the didehydro-CDPs had no activity, indicating that dehydrogenation at α,β-positions of both amino acid residues in CDPs is required for cytotoxicity. Based on the above results, we speculated that a tetradehydro-CDP prepared from a didehydro-CDP exhibiting cytotoxicity might be a potent cytotoxic compound. Dehydrophenylahistin synthesized by this enzyme system from (-)-phenylahistin, which was recently reported to be a new cell cycle inhibitor, exhibited 1000 times higher inhibitory activity toward the first cleavage of sea urchin embryo than (-)-phenylahistin, and thus, would be a promising lead compound for antitumor agents.

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Production of Bioactive Compounds by Microbial Diketopiperazine-Metabolizing Enzymes

KANZAKI HIROSHI

79(3), 71-77 ( 3 )   71 - 77   2001

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iketopiperazines(DKPs)and their derivatives are widely distributed in nature as secondary metabolites.Although some dehydroDKPs are known as cell cycle inhibitors, their effective synthesis has not been reported. We found that the cell-free extract from an albonoursin-producing actinomycete, Streptomyces albulus KO23, catalyzed the conversion of cyclo(Leu-Phe)to albonoursin. This is the first report on the dehydrogenation of amino acid residues at the α, β-positions in DKPs. Furthermore, this enzyme system enabled us to synthesize several didehydro- and tetradehydro- DKPs from the corresponding DKPs. Among the dehydroDKPs prepared, dehydrophenylahistin from (-)-phenylahistin, which was recently reported to be a new cell cycle inhibitor, exhibited 1000 times higher inhibitory activity toward the first clevage of sea urchin embrvo than (-)-phenylahistin, and would thus be a promising lead compound for antitumor agents. Agrobacterium radiobacter NM 5-3 isolated from soil hydrolyzed CGL to from dipeptides(i.e., Leu-Gly and Gly-Leu)and amino acids(i.e., Leu and Gly). This CGL hydrolysis was catalyzed by two distinct enzymes, CGLase and dipeptidase, which were separated by anion-exchange column chromatography. The CGLase was found to catalyze the hydrolysis of CGDL, CGG, CAG, and CDAG. On the other hand, the dipeptidase exhibited L-specific substrate specificity.

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Effective production of dehydro cyclic dipeptide albonoursin exhibiting pronuclear fusion inhibitory activity II. Biosynthetic and bioconversion studies

Hiroshi Kanzaki, Daisuke Imura, Teruhiko Nitoda, Kazuyoshi Kawazu

Journal of Antibiotics   53 ( 1 )   58 - 62   2000

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Albornoursin production was greatly enhanced when cycle (r-Leu-L-Phe) (CFL), a tetrahydro derivative of albonoursin, was added to the 2-day culture of an albonoursin-producing actinomycete, Streptomyces albulus KO-23. The increase in albonoursin production paralleled the amount of CFL added. Furthermore, the resting cells of the strain catalyzed the bioconversion of CFL to albonoursin. The optimum pH and temperature for the conversion were found to be pH 10.0 and 50°C. The feeding experiments and the resting-cell reactions revealed that albonoursin is biosynthesized by dehydrogenation of CFL in the actinomycete. This is the first report for a dehydrogenation of amino acid residues at the α,β-positions in cyclic dipeptides.

DOI： 10.7164/antibiotics.53.58

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A novel microbial enzyme system for hydrolyzing a cyclic dipeptide, cyclo(Gly-Leu)

Kanzaki Hiroshi, Miyoshi Kazuyuki, Mizuta Naoki, Nitoda Teruhiko

12   210 - 210   2000

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Improved bioassay method for Spodoptera litura chitinase inhibitors using a colloidal chitin powder with a uniform particle size as substrate

T Nitoda, H Kurumatani, H Kanzaki, K Kawazu

PESTICIDE SCIENCE   55 ( 5 )   563 - 565   1999.5

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A previously reported bioassay method for Spodoptera litura chitinase inhibitors has been improved by use of colloidal chitin powder with a uniform particle size. This improvement made the assay four times more sensitive. Detection of three active supernatants by screening of supernatants and cell extracts from 135 fermentation broths has proved the efficiency of this improved method. (C) 1999 Society of Chemical Industry.

DOI： 10.1002/(SICI)1096-9063(199905)55:5<563::AID-PS972>3.0.CO;2-#

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Enzymatic dehydrogenation of cyclo(L-Phe-L-Leu) to a bioactive derivative, albonoursin

H Kanzaki, D Imura, T Nitoda, K Kawazu

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC   6 ( 3 )   265 - 270   1999.3

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The cell-free extract of Streptomyces sp. KO-2388, an albonoursin-producing strain, was found to catalyze the conversion of cyclo(L-Phe-L-Leu) to albonoursin. The conversion activity was simply determined by measuring the increase in ultraviolet (UV) absorption of the reaction mixture at 317 nm, lambda(max) (epsilon 25,400) of albonoursin, where cyclo(L-Phe-L-Leu) had no absorption. The optimum pH and temperature of this bioconversion using the cell-free extract were determined to be pH 8.0-9.5 and 60 degrees C, respectively. Under the optimum conditions, 620 mg/l of albonoursin was obtained with a conversion ratio of 62% after 24 h incubation. (C) 1999 Elsevier Science B.V. All rights reserved.

DOI： 10.1016/S1381-1177(98)00079-4

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Inhibition of plant transformation by phytolaccoside b from phytolacca americana callus

Hiroshi Kanzaki, Toshihiko Kagemori, Yoko Yamachika, Teruhiko Nitoda, Kazuyoshi Kawazu

Bioscience, Biotechnology and Biochemistry   63 ( 9 )   1657 - 1659   1999.1

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The newly established GUS expression bioassay on the callus extracts of 22 species of plants revealed that the methanol extract of Phytolacca americana callus had the most potent inhibitory activity against agrobacterial plant transformation. A triterpene glycoside phytolaccoside B was isolated from the extract as a genuine plant transformation inhibitor having neither antiagrobacterial nor phytotoxic activity. This compound is promising for use as a biochemical probe for studies on the plant transformation mechanism. © 1999, Taylor &amp
Francis Group, LLC. All rights reserved.

DOI： 10.1271/bbb.63.1657

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Effective production of dehydro cyclic dipeptide albonoursin exhibiting pronuclear fusion inhibitory activity. I. Taxonomy and fermentation

Hiroshi Kanzaki, Daisuke Imura, Reiko Sashida, Akio Kobayashi, Kazuyoshi Kawazu

Journal of Antibiotics   52 ( 11 )   1017 - 1022   1999

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Strain KO-23, an actinomycete producing albonoursin as well as streptopyrone, was identified as Streptomyces albulus by morphological and biochemical studies. Fermentation conditions for albonoursin, a dehydro cyclic dipeptide exhibiting a pronounced inhibitory activity toward pronuclear fusion of sea urchin eggs, were optimized. Under the optimum conditions, the actinomycete produced 16 mg/liter of albonoursin, 30 times higher than that in the original culture. The cells cultivated under these conditions highly express biosynthetic enzymes for albonoursin, and thus are available for biosynthetic studies of dehydro cyclic peptides.

DOI： 10.7164/antibiotics.52.1017

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病原体を接種して萎凋させたアカマツ実生からの病原体の再分離およびマツノザイセンチュウの分離系統間の病原性の差異．

河津一儀, 金子昇, 平岡享子, 山下秀昭, 神崎浩

岡山大学農学部学術報告   88   1 - 6   1999

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Other Link： http://ousar.lib.okayama-u.ac.jp/11038

新規の環状ジペプチド脱水素酵素とその活性測定法の確立．

神崎浩, 赤澤和美, 井村大輔, 仁戸田照彦

岡山大学農学部学術報告   1999

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Microbial hyrodolysis of cyclo(Gly-Leu)

Kanzaki Hiroshi, Mizuta Naoki, Miyoshi Kazuyuki, Nitoda Teruhiko

11   202 - 202   1999

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Calophyllum inophyllumの抗HIV活性成分inophyllum A,B,C,D,E,Pの液体クロマトグラフィー・による分析法の確立

河津 一儀, 仁戸田 照彦, 神崎 浩

岡山大学農学部学術報告   87   13 - 16   1998.2

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Other Link： http://ousar.lib.okayama-u.ac.jp/11052

Novel bioactive oxazolomycin isomers produced by streptomyces albus JA3453

Hiroshi Kanzaki, Ken-Ichi Wada, Teruhiko Nitoda, Kazuyoshi Kawazu

Bioscience, Biotechnology and Biochemistry   62 ( 3 )   438 - 442   1998

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Two novel oxazolomycin isomers, oxazolomycins B (2) and C (3), were isolated from the fermentation broth of an oxazolomycin-producing strain, Streptomyces albus JA3453. Both compounds are geometrical isomers of oxazolomycin (1), the configurations of their triene moieties being (4′E, 6′E, 8′E) (2) and (4′Z, 6′E, 8′E) (3) while that of oxazolomycin (1) is (4′Z, 6′Z, 8′E). Compounds 2 and 3 exhibited potent inhibitory activity against crown gall formation with the same MIC (0.8 μg/disk) as oxazolomycin. Compounds 2 and 3 showed no antibacterial activity against Agrobacterium tumefaciens, in contrast to oxazolomycin which has specific anti-A. tumefaciens activity. © 1998, Taylor &amp
Francis Group, LLC. All rights reserved.

DOI： 10.1271/bbb.62.438

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Improved bioassay method for plant transformation inhibitors

Hiroshi Kanzaki, Toshihiko Kagemori, Satomi Asano, Kazuyoshi Kawazu

Bioscience, Biotechnology and Biochemistry   62 ( 12 )   2328 - 2333   1998

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A convenient and quantitative bioassay method for evaluating the efficiency of plant transformation by Agrobacterium tumefaciens is important to search plant transformation inhibitors, possible biochemical probes for study on its mechanism. Our previously reported method, in which the plant transformation had been detected by the expression of β-glucuronidase in transformed plants, was improved. The difference between the previous and the improved methods is the use of suspension-cultured cells of Ageratum conyzoides as the host plant instead of Nicotiana tabacum BY-2
this alteration of the host enabled us to measure the β-glucuronidase activity in plant cells not only fluorometrically but also colorimetrically. The enzyme activity expressed in the cells of A. conyzoides was nearly 100 times higher than that of N. tabacum BY-2, and was enough for detection by colorimetric measurement. The method, therefore, is useful for a convenient determination of inhibitory activity against plant transformation. © 1998, Taylor &amp
Francis Group, LLC. All rights reserved.

DOI： 10.1271/bbb.62.2328

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Microbial hydrolysis of diketopiperazines: Different types of diketopiperazine-assimilating bacteria

H Kanzaki, S Oda, A Kobayashi, K Kawazu

JOURNAL OF FERMENTATION AND BIOENGINEERING   83 ( 4 )   386 - 388   1997

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Arthrobacter sp. 1-3-1 and a coryneform rod bacterium, strain T-1-3-Y, which assimilate cyclo(Gly-Gly) and cyclo(Gly-L-Tyr) at high rates, respectively, were isolated from sell. Both bacteria exhibit diketopiperazine-hydrolyzing activity intracellularly in contrast to the extracellular cyclo(Gly-Gly) hydrolase reported previously. Arthrobacter sp. 1-3-1 shows a much broader substrate specificity than strain T-1-3-Y, indicating the diversity of diketopiperazine hydrolysis in nature.

DOI： 10.1016/S0922-338X(97)80147-X

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Inhibitory effect of curromycins and their esters on plant transformation

Hiroshi Kanzaki, Toshitsune Ichioka, Akio Kobayashi, Kazuyoshi Kawazu

Bioscience, Biotechnology and Biochemistry   60 ( 9 )   1535 - 1537   1996

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Curromycins A and B, antibiotics specific to Agrobacterium tumefaciens, inhibited crown gall formation on potato tubers. Their esters showed potent inhibitory activity against crown gall formation without any antibacterial activity. The change in biological activity of curromycins by simple esterification was similar to our previous observation in oxazolomycin. Curromycin esters are possible chemical probes to study the mechanism for plant transformation. © 1996, Taylor &amp
Francis Group, LLC. All rights reserved.

DOI： 10.1271/bbb.60.1535

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An effective method of screening glucose-rich microbial culture filtrates for insect trehalase inhibitors

Hiroshi Kanzaki, Takafumi Nuhama, Akio Kobayashi, Kazuyoshi Kawazu

Bioscience, Biotechnology and Biochemistry   59 ( 3 )   398 - 400   1995

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Trehalase inhibitors are promising as a specific insect growth regulator. Microbial culture filtrates are a good source of bioactive compounds, but some of them retain a significant amount of glucose, a major component of the culture medium, which makes it difficult to detect trehalase inhibitors because of high blank values for the glucose determination. To find a variety of trehalase inhibitors in glucose-rich microbial culture filtrates, an effective method for removing glucose by enzymatic conversion prior to a routine trehalase-inhibitory assay was devised. Conversion with glucose oxidase and catalase could completely remove 10mg/ml of glucose, and a wide variety of microbial culture filtrates with high glucose content could then be subjected to the routine bioassay. This method can also be applied to screen inhibitors for other enzymes whose activity is assayed by the amount of glucose formed. © 1995 Taylor &amp
Francis Group LLC.

DOI： 10.1080/bbb.59.398

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A novel bioassay method for inhibitors against plant transformation

Kanzaki Hiroshi, Toyoshima Hiroto, Kobayashi Akio, Kawazu Kazuyoshi

Bioscience, Biotechnology and Biochemistry   58 ( 3 )   531 - 534   1994.3

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A rapid and quantitative bioassay method for inhibitors of plant transformation by Agrobacterium tumefaciens with an intron-GUS binary vector was devised as an alternative method to the time-consuming potato tuber disk assay. Among several host plants tested, tobacco BY-2 suspension cells were the most preferable for this GUS expression assay. Furthermore, as the phytotoxicity of the test material, if any, is apparent from the growth inhibition of BY-2 suspension cells, this method can exclude phytotoxic com pounds.

DOI： 10.1271/bbb.58.531

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A Novel Bioassay Method for Inhibitors of Plant Transformation

Kanzaki Hiroshi, Toyoshima Hiroto, Kobayashi Akio, Kawazu Kazuyoshi

Bioscience, biotechnology, and biochemistry   58 ( 3 )   531 - 534   1994.3

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A rapid and quantitative bioassay method for inhibitors of plant transformation by Agrobacterium tumefaciens with an intron-GUS binary vector was devised as an alternative method to the time-consuming potato tuber disk assay. Among several host plants tested, tobacco BY-2 suspension cells were the most preferable for this GUS expression assay. Furthermore, as the phytotoxicity of the test material, if any, is apparent from the growth inhibition of BY-2 suspension cells, this method can exclude phytotoxic com pounds.

DOI： 10.1271/bbb.58.531

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47 THE ROLE OF PEROXIDASE IN THE CHEMICAL DEFENCE OF PLANTS : A NOVEL PEROXIDASE INHIBITOR AND A NEW TYPE OF BIOACTIVE PHENOLICS PRODUCED BY PEROXIDASE

Kobayashi A, Koguchi Y, Kanzaki H, Kajiyama S, Kawazu K

天然有機化合物討論会講演要旨集   ( 35 )   361 - 368   1993.9

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Plants induce varied resistance-response toward microbial challenge. In order to establish an infection, pathogenic fungi must break such defense barriers as lignin, phytoalexins, and hydrolytic enzymes. At the early stage of infection, POD (peroxidase) activity is enhanced dramatically. POD and lignin accumulates at the infected site and then protects from further fungal invasion. The suppression of lignin deposition at the site might be of advantage to susceptible pathogenic fungi. We, therefore, conducted a comprehensive screening to obtain POD inhibitors from fungal cultures and a potent radical scavenger named ST-1 was isolated from a fungus, and its chemical structure was elucidated to be 1,3-dihydro-4,5,6-trihydroxy-1,3-dimethoxy-7-methylisobenzofuran by a combination of chemical modification and spectroscopic techniques. ST-1 effectively scavenged oxygen radicals and also suppressed the phytoalexin accumulation in kidney bean. These results suggested that such a mechanism can be enumerated as one of significant defense systems intervening plants and microbes. On the other hand, the POD, activated upon pathogenic challenge, could convert common plant phenolics into bioactive compounds which interfered with pathogen and insect attacks. This idea prompted us to examine the possibility. Guaiacol and other phenols were chosen as model substrates for the enzyme reaction system, and several products with novel structures were confirmed to have unique biological activities. This paper deals with the chemical structures of a novel radical scavenger (ST-1) and the POD products with anti-microbial activities and phytotoxicities.

DOI： 10.24496/tennenyuki.35.0_361

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Bisanthraquinones, Inhibitors of Plant Transformation

Hiroshi Kanzaki, Goro Kawabata, Akio Kobayashi, Kazuyoshi Kawazu

Bioscience, Biotechnology, and Biochemistry   57 ( 12 )   2104 - 2106   1993

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A potato tuber disk assay of culture broths which had been confirmed to show neither antibacterial nor phytotoxic activity resulted in the discovery of a novel type of crown gall formation inhibitors, julimycin B-II and julichrome Q1.3. These two bisanthraquinones, products of Streptomyces sp. TM-71, inhibited crown gall formation on potato tuber disks at a minimum inhibitory dose of 1.6μg/disk without affecting the growth of Agrobacterium tumefaciens or the germination of alfalfa seeds. © 1993, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.

DOI： 10.1271/bbb.57.2104

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Oxazolomycin Esters, Specific Inhibitors of Plant Transformation

Kazuyoshi Kawazu, Goro Kawabata, Satoru Kawai, Akio Kobayashi, Hiroshi Kanzaki

Bioscience, Biotechnology and Biochemistry   56 ( 9 )   1382 - 1385   1992

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Oxazolomycin diacetate, dipropionate, monobutyrate and dibutyrate were derived from oxazolomycin, a product of Streptomyces sp. KBFP-2025. These esters were potent inhibitors of crown gall formation on potato tuber disks upon infection with Agrobacterium tumefaciens. They showed neither antibacterial nor phytotoxic activity, whereas oxazolomycin showed both antibacterial and phytotoxic activities. Further, they had no inhibitory activity against A. tumefaciens on the potato tuber disk. The inhibitory activity of these esters against crown gall formation seems to be due to specific inhibition of the transformation of plants with A. tumefaciens. © 1992, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.

DOI： 10.1271/bbb.56.1382

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Preparation and identification of the alfalfa elicitor from brown algae laminaran.

KOBAYASHI Akio, TAI Akihiro, KANZAKI Hiroshi, KAWAZU Kazuyoshi

Chemical Regulation of Plants   26 ( 2 )   222 - 222   1991.12

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Production of Benzoylformic Acid from Phenylglycine by Saccharomycopsis lipolytica

Hiroshi Kanzaki, Atsuhiko Isobe, Yoshikazu Izumi, Hideaki Yamada

Agricultural and Biological Chemistry   54 ( 8 )   2101 - 2105   1990

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Microbial production of benzoylformic acid (BF), which can be used as a substrate of enzymatic synthesis of (R)-(—)-mandelic acid, was investigated. Among 145 strains of yeasts and actinomycetes, Saccharomycopsis lipolytica (IAM 4964) was the best producer of BF from DL-phenylglycine (DL-PG). Culture conditions for BF production by the organism were optimized. When 0.2 % fructose as a carbon source and 0.7% Bacto-tryptone as a nitrogen source were used in the presence of 4 % dl-PG, 14.5 mg/ml of BF was produced (about 37 % molar yield) in 4 days of cultivation. BF was synthesized from the L-form of PG, but not from the D-form. The BF was isolated from culture broth in a crystalline form and physicochemically identified. © 1990, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.

DOI： 10.1271/bbb1961.54.2101

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Characterization of crystalline formate dehydrogenase from Candida methanolica

Yoshikazu IZUMI, Hiroshi KANZAKI, Shigeru MORITA, Hideaki FUTAZUKA, Hideaki YAMADA

European Journal of Biochemistry   182 ( 2 )   333 - 341   1989

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The crystalline formate dehydrogenase from Candida methanolica, which showed the highest specific activity (7.52 U/mg) so far reported, was characterized in detail. The enzyme is a dimer composed of identifical subunits, each containing one SH group related to the catalytic activity. The molecular mass of the enzyme is about 82–86 kDa. The Km values were found to be 3.0 mM for formate and 0.11 mM for NAD+. Even if the enzyme was incubated at pH 6.5–9.5 or at 55°C, the activity remained at 100%. Hg2+, Ni2+, NaCN, NaN3 and p‐chloromercuribenzoate strongly inhibited the enzyme activity, while the enzyme showed relatively high resistance to various chelating agents. The amino acid composition and some other physicochemical properties of the enzyme were studied. Immunological studies revealed that formate dehydrogenases of methanol‐utilizing yeasts immunologically more or less resemble each other, but differ from those of methanol‐utilizing bacteria. Furthermore, yeast formate dehydrogenases can be immunologically classified into three types: (a) the Candida type, (b) the Torulopsis/Hansenula/Pichia type and (c) the formaldehyde‐resistant yeast type. For simple and large‐scale preparation of the enzyme for practical use, treatment of cells of C. methanolica with the commercial cationic detergent, ‘Benzalkonium’ cation, is useful: the total and specific activities of the enzyme are 1.17‐fold and 3.10‐fold higher than those of the crude cell‐free extract, respectively. Copyright © 1989, Wiley Blackwell. All rights reserved

DOI： 10.1111/j.1432-1033.1989.tb14835.x

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Purification and characterization of cystathionine γ‐synthase type II from Bacillus sphaericus

Hiroshi KANZAKI, Michihiko KOBAYASHI, Toru NAGASAWA, Hideaki YAMADA

European Journal of Biochemistry   163 ( 1 )   105 - 112   1987

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Cystathionine γ‐synthase type II, which catalyzes l‐cystathionine synthesis from O‐acetyl‐l‐homoserine and l‐cysteine was purified from Bacillus sphaericus (IFO 3536) in seven steps. The purified enzyme appeared to be homogeneous by the results of polyacrylamide electrophoresis and ampholyte electrofocusing. The enzyme is a typical pyridoxal‐P dependent enzyme, has a molecular mass of 165 kDa and consists of four subunits identical in molecular mass. The enzyme catalyzed the γ‐replacement reaction and the elimination reaction was hardly detected even when a large amount of enzyme was added. In the replacement reaction, O‐acetyl‐l‐homoserine and the following thiol compounds: L and d‐cysteine, L and d‐homocysteine, sodium sulfide, various alkyl and aryl mercaptans, acted as the most suitable substrate to produce l‐cystathionine and the corresponding S‐substituted l‐homocysteine derivatives. Copyright © 1987, Wiley Blackwell. All rights reserved

DOI： 10.1111/j.1432-1033.1987.tb10742.x

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Purification and characterization of cystathionine γ‐synthase type II from Bacillus sphaericus

Hiroshi KANZAKI, Michihiko KOBAYASHI, Toru NAGASAWA, Hideaki YAMADA

European Journal of Biochemistry   163 ( 1 )   105 - 112   1987

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Cystathionine γ‐synthase type II, which catalyzes l‐cystathionine synthesis from O‐acetyl‐l‐homoserine and l‐cysteine was purified from Bacillus sphaericus (IFO 3536) in seven steps. The purified enzyme appeared to be homogeneous by the results of polyacrylamide electrophoresis and ampholyte electrofocusing. The enzyme is a typical pyridoxal‐P dependent enzyme, has a molecular mass of 165 kDa and consists of four subunits identical in molecular mass. The enzyme catalyzed the γ‐replacement reaction and the elimination reaction was hardly detected even when a large amount of enzyme was added. In the replacement reaction, O‐acetyl‐l‐homoserine and the following thiol compounds: L and d‐cysteine, L and d‐homocysteine, sodium sulfide, various alkyl and aryl mercaptans, acted as the most suitable substrate to produce l‐cystathionine and the corresponding S‐substituted l‐homocysteine derivatives. Copyright © 1987, Wiley Blackwell. All rights reserved

DOI： 10.1111/j.1432-1033.1987.tb10742.x

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Insight into the active site of Streptomyces cystathionine γ-lyase based on the results of studies on its substrate specificity

KANZAKI H.

Biochim. Biophys. Acta   913   45 - 50   1987

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Highly efficient production of l-cystathionine from O-succinyl-l-homoserine and l-cysteine by Streptomyces cystathionine γ-lyase

Hiroshi Kanzaki, Toru Nagasawa, Hideaki Yamada

Applied Microbiology and Biotechnology   25 ( 2 )   97 - 100   1986

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Language：English   Publisher：Springer-Verlag  

Utilizing the γ-replacement reaction of Streptomyces cystathionine γ-lyase (EC 4.4.1.1.), an efficient production method for l-cystathionine has been established. Under optimal conditions, 50 mM l-cystathionine was synthesized from 50 mM O-succinyl-l-homoserine and 50 mM l-cysteine, added in four stages to the reaction mixture, with a substrate conversion rate of 100%. This productivity (11 gl-1 of reaction mixture) is about 3.5 times higher than that with l-homoserine and l-cysteine as substrates. © 1986 Springer-Verlag.

DOI： 10.1007/BF00250516

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