Xanthomonas oryzae、Aspergillus oryzae

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/08/04 20:10:59」(JST)

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Aspergillus oryzae (Chinese: 麴菌, 麴霉菌, 曲霉菌, pinyin: qū meí jūn; Japanese: 麹, kōji, or 麹菌, kōji-kin, Korean: 누룩균, nurukgyun or 누룩곰팡이 nuruk-gompang-i) is a filamentous fungus (a mold). It is used in Chinese, Korean, and Japanese cuisine to ferment soybeans. It is also used to saccharify rice, other grains, and potatoes in the making of alcoholic beverages such as huangjiu, sake, makgeolli and shōchū. The domestication of A. oryzae occurred at least 2000 years ago.^[2] A. oryzae is used for the production of rice vinegars.

Dr. Eiji Ichishima of Tohoku University called the kōji fungus a "national fungus" (kokkin) in the journal of the Brewing Society of Japan, because of its importance not only for making the koji for sake brewing, but also for making the koji for miso, soy sauce and a range of other traditional Japanese foods. His proposal was approved at the society's annual meeting in 2006.^[3]

"Red kōji-kin" is a separate species, Monascus purpureus.

History of koji

300 BCE – A. oryzae (qu, pronounced "chew") is first mentioned in the Zhouli (Rites of the Zhou dynasty) in China. Its development is a milestone in Chinese food technology, for it provides the conceptual framework for three major fermented soy foods: soy sauce, jiang / miso, and fermented black soybeans, not to mention grain-based wines (including Japanese sake) and li (the Chinese forerunner of Japanese amazake).^[4]

Properties desirable in sake brewing and testing

The following properties of A. oryzae strains are important in rice saccharification for sake brewing:^[5]

Growth: rapid mycelial growth on and into the rice kernels
Enzymes: strong secretion of amylases (α-amylase and glucoamylase); some carboxypeptidase; low tyrosinase
Aesthetics: pleasant fragrance; accumulation of flavoring compounds
Color: low production of deferriferrichrome (a siderophore), flavins, and other colored substances

Varieties used for shōchū making

There are three varieties of kōji mold used for making shōchū, each with distinct characteristics.^[6]^[7]^[8]

White. Discovered at the beginning of the Taishō period when natural mutation and separation of some black kōji to white was observed. This effect was researched and white kōji was successfully grown independently. White kōji is easy to cultivate and its enzymes promote rapid saccharization; as a result it is used to produce most shōchū today. It gives rise to a drink with a refreshing, gentle, sweet taste.
Black. Mainly used in Okinawa to produce Awamori. It produces plenty of citric acid which helps to prevent the souring of the moromi. Of all three kōji it most effectively extracts the taste and character of the base ingredients, giving its shōchū a rich aroma with a slightly sweet, mellow taste. Its spores disperse easily, covering production facilities and workers' clothes in a layer of black. Such issues led to it falling out of favour, but due to the development of New Kuro-kōji (NK-kōji) in the mid-1980s,^[9] interest in black kōji resurged amongst honkaku shōchū makers because of the depth and quality of the taste it produced. Several popular brands now explicitly state they use black kōji on their labels.
Yellow. Used to produce sake, and at one time all honkaku shōchū. However yellow kōji is extremely sensitive to temperature; its moromi can easily sour during fermentation. This makes it difficult to use in warmer regions such as Kyūshū, and gradually black and white kōji became more common. Its strength is that it gives rise to a rich, fruity refreshing taste, so despite the difficulties and great skill required it is still used by some manufacturers. It is popular amongst young people and women who previously had no interest in typically strong potato shōchū, playing a rôle in its recent revival.

Genome

Initially kept secret, the A. oryzae genome was released by a consortium of Japanese biotechnology companies^[10] in late 2005.^[11] The eight chromosomes together comprise 37 million base pairs and 12 thousand predicted genes. The genome of A. oryzae is thus one-third larger than that of two related Aspergillus species, the genetics model organism A. nidulans and the potentially dangerous A. fumigatus.^[12] Many of the extra genes present in A. oryzae are predicted to be involved in secondary metabolism. The sequenced strain isolated in 1950 is called RIB40 or ATCC 42149; its morphology, growth, and enzyme production are typical of strains used for sake brewing.^[2]

Use in biotechnology

Resveratrol can be produced from its glucoside piceid through the process of fermentation by A. oryzae.^[13]

In fiction

A. oryzae is a supporting character (of sorts) in the manga series Moyasimon: Tales of Agriculture and its anime adaptation.

References

^ Index Fungorum
^ ^a ^b Rokas, A. (2009). "The effect of domestication on the fungal proteome". Trends in genetics : TIG 25 (2): 60–63. doi:10.1016/j.tig.2008.11.003. PMID 19081651. edit
^ http://www.tokyofoundation.org/en/series/japanese-traditional-foods/vol.-10-koji-an-aspergillus
^ Shurtleff, W.; Aoyagi, A. History of Koji - Grains and/or Soybeans Enrobed with a Mold Culture (300 BCE to 2012). Lafayette, California: Soyinfo Center. 660 pp. (1,560 references; 142 photos and illustrations, Free online)
^ Kitamoto, Katsuhiko (2002). "Molecular Biology of the Koji Molds". Advances in Applied Microbiology. Advances in Applied Microbiology 51: 129–153. doi:10.1016/S0065-2164(02)51004-2. ISBN 9780120026531. PMID 12236056. Retrieved 2008-01-03.
^ "In-depth". Retrieved 2007-01-24. (Japanese)
^ "What is Shochu?". Retrieved 2007-01-24.
^ "Other terminology relating to Shochu and Awamori". Retrieved 2007-01-27. (Japanese)
^ "Shochu Circle". Retrieved 2007-12-11.
^ Goffeau, André (December 2005). "Multiple moulds". Nature 438 (7071): 1092–1093. doi:10.1038/4381092b. PMID 16371993.
^ Machida, Masayuki et al. (December 2005). "Genome sequencing and analysis of Aspergillus oryzae". Nature 438 (7071): 1157–1161. doi:10.1038/nature04300. PMID 16372010.
^ Galagan, James E. et al. (December 2005). "Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae". Nature 438 (7071): 1105–1115. doi:10.1038/nature04341. PMID 16372000.
^ Wang, H.; Liu, L.; Guo, Y. -X.; Dong, Y. -S.; Zhang, D. -J.; Xiu, Z. -L. (2007). "Biotransformation of piceid in Polygonum cuspidatum to resveratrol by Aspergillus oryzae". Applied Microbiology and Biotechnology 75 (4): 763–768. doi:10.1007/s00253-007-0874-3. PMID 17333175. edit

External links

Sake World's description of koji
Aspergillus oryzae genome from the Database of Genomes Analysed at NITE (DOGAN)
Koji, an Aspergillus, by Fujita, Chieko, Tokyo Foundation

UpToDate Contents

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English Journal

Optimisation of soy flour fermentation parameters to produce β-glucosidase for bioconversion into aglycones.

Handa CL1, Couto UR1, Vicensoti AH1, Georgetti SR2, Ida EI3.Author information 1Departamento de Ciência e Tecnologia de Alimentos, Universidade Estadual de Londrina, 86057-970 Londrina, Paraná, Brazil.2Departamento de Ciências Farmacêuticas, Universidade Estadual de Londrina, 86057-970 Londrina, Paraná, Brazil.3Departamento de Ciência e Tecnologia de Alimentos, Universidade Estadual de Londrina, 86057-970 Londrina, Paraná, Brazil. Electronic address: elida@uel.br.AbstractThe solid state fermentation (SSF) parameters of defatted soybean flour (DSF) with Aspergillus oryzae IOC 3999/1998 or Monascus purpureus NRRL 1992 was evaluated using a rotational central composite experimental design to optimise the production of β-glucosidase and convert glycosidic isoflavones in aglycones. Variables investigated were initial pH of DSF, volume of water added to 10 g of DSF and incubation temperature. β-Glucosidase activity was measured using the synthetic substrate, p-nitrophenyl-β-D-glucoside. The content of isoflavones was determinate by ultra performance liquid chromatography. The highest production of β-glucosidase for both strains occurred when adding 10 mL of water to the DSF, incubating at 30 °C and using 6.0 as the initial DSF pH. A. oryzae IOC 3999/1998 expressed β-glucosidase activity at 10.7 times higher than M. purpureus NRRL 1992. The DSF fermentation was more efficient in converting isoflavones with M. purpureus NRRL 1992.
Food chemistry.Food Chem.2014 Jun 1;152:56-65. doi: 10.1016/j.foodchem.2013.11.101. Epub 2013 Nov 27.
The solid state fermentation (SSF) parameters of defatted soybean flour (DSF) with Aspergillus oryzae IOC 3999/1998 or Monascus purpureus NRRL 1992 was evaluated using a rotational central composite experimental design to optimise the production of β-glucosidase and convert glycosidic isoflavones i
PMID 24444906

Molecular modeling of protein-protein interaction to decipher the structural mechanism of nonhost resistance in rice.

Bahadur RP1, Basak J.Author information 1a Department of Biotechnology , Indian Institute of Technology , Kharagpur , 721302 , India .AbstractNonhost resistance (NHR) is the most common and durable form of plant resistance to disease-causing organisms. A successful example of NHR is the cloning of a maize R gene Rxo1 in rice and validating its function in conferring bacterial streak resistance in transgenic rice lines. In order to understand the structural mechanism of NHR in rice, we built the model of the protein-protein interaction between the encoded Rxo1 (RXO1) and AvrRXO1 (avirulence protein of rice pathogen, Xanthomonas oryzae pv. oryzicola). Interestingly, although a RXO1 homolog in rice (RHR) is present, it does not interact with AvrRXO1 in nature. We have confirmed that the specificity of RXO1-AvrRXO1 interaction originates from the structured leucine rich repeat (LRR) domain of RXO1, facilitating the recognition process, while the absence of such ordered LRR region makes RHR unfavorable to recognize AvrRXO1. We postulate that the RXO1-AvrRXO1 complex formation is a three step process where electrostatic interactions, shape complementarity and short-range interactions play an important role. The presence of the structural and physicochemical properties essential for the protein-protein recognition process empowers RXO1 to mediate NHR, which the host protein RHR lacks and consequently loses its specificity to bind with AvrRXO1. To the best of our knowledge, this is the first report on the understanding of NHR in rice from the structural perspective of protein-protein interaction.
Journal of biomolecular structure & dynamics.J Biomol Struct Dyn.2014 Apr;32(4):669-81. doi: 10.1080/07391102.2013.787370. Epub 2013 May 10.
Nonhost resistance (NHR) is the most common and durable form of plant resistance to disease-causing organisms. A successful example of NHR is the cloning of a maize R gene Rxo1 in rice and validating its function in conferring bacterial streak resistance in transgenic rice lines. In order to underst
PMID 23659345

Extracellular matrix-associated proteome changes during non-host resistance in citrus-Xanthomonas interactions.

Swaroopa Rani T1, Podile AR.Author information 1Department of Plant Sciences, School of Life Sciences, University of Hyderabad, Hyderabad, 500 046, Andhra Pradesh, India.AbstractNon-host resistance (NHR) is a most durable broad-spectrum resistance employed by the plants to restrict majority of pathogens. Plant extracellular matrix (ECM) is a critical defense barrier. Understanding ECM responses during interaction with non-host pathogen will provide insights into molecular events of NHR. In this study, the ECM-associated proteome was compared during interaction of citrus with pathogen Xanthomonas axonopodis pv. citri (Xac) and non-host pathogen Xanthomonas oryzae pv. oryzae (Xoo) at 8, 16, 24 and 48 h post inoculation. Comprehensive analysis of ECM-associated proteins was performed by extracting wall-bound and soluble ECM components using both destructive and non-destructive procedures. A total of 53 proteins was differentially expressed in citrus-Xanthomonas host and non-host interaction, out of which 44 were identified by mass spectrometry. The differentially expressed proteins were related to (1) defense-response (5 pathogenesis-related proteins, 3 miraculin-like proteins (MIR, MIR1 and MIR2) and 2 proteases); (2) enzymes of reactive oxygen species (ROS) metabolism [Cu/Zn superoxide dismutase (SOD), Fe-SOD, ascorbate peroxidase and 2-cysteine-peroxiredoxin]; (3) signaling (lectin, curculin-like lectin and concanavalin A-like lectin kinase); and (4) cell-wall modification (α-xylosidase, glucan 1, 3 β-glucosidase, xyloglucan endotransglucosylase/hydrolase). The decrease in ascorbate peroxidase and cysteine-peroxiredoxin could be involved in maintenance of ROS levels. Increase in defense, cell-wall remodeling and signaling proteins in citrus-Xoo interaction suggests an active involvement of ECM in execution of NHR. Partially compromised NHR in citrus against Xoo, upon Brefeldin A pre-treatment supported the role of non-classical secretory proteins in this phenomenon.
Physiologia plantarum.Physiol Plant.2014 Apr;150(4):565-79. doi: 10.1111/ppl.12109. Epub 2013 Oct 26.
Non-host resistance (NHR) is a most durable broad-spectrum resistance employed by the plants to restrict majority of pathogens. Plant extracellular matrix (ECM) is a critical defense barrier. Understanding ECM responses during interaction with non-host pathogen will provide insights into molecular e
PMID 24117905

Japanese Journal

Confirming a major QTL and finding additional loci responsible for field resistance to brown spot (Bipolaris oryzae) in rice

Sato Hiroyuki,Matsumoto Kengo,Ota Chihiro [他]
Breeding science 65(2), 170-175, 2015-03
NAID 40020417864

イネ各種菌核病を引き起こすRhizoctonia及びScleotium属菌の菌核発芽様式

清水稔,荒川征夫,稲垣公治
名城大学農学部学術報告 = Scientific reports of the Faculty of Agriculture, Meijo University (51), 9-15, 2015-03
NAID 40020411597

A putative transcription factor Gf.BMR1 in Grifola frondosa, the homolog of BMR1 in Bipolaris oryzae, was strongly induced by near-ultraviolet light and blue light

Kurahashi Atsushi,Shimoda Takafumi,Sato Masayuki [他]
Mycoscience : official journal of the Mycological Society of Japan 56(2), 177-182, 2015-03
NAID 40020402995

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拡張検索	「Aspergillus oryzae」

「Aspergillus oryzae」

Aspergillus oryzae
	A. oryzae growing on rice to make koji
Scientific classification
Domain:	Eukarya
Kingdom:	Fungi
Division:	Ascomycota
Class:	Eurotiomycetes
Order:	Eurotiales
Family:	Trichocomaceae
Genus:	Aspergillus
Species:	A. oryzae
Binomial name
	Aspergillus oryzae; (Ahlburg) E. Cohn

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関: aspergilli

[1] Index Fungorum

[TiG2009-2] Rokas, A. (2009). "The effect of domestication on the fungal proteome". Trends in genetics : TIG 25 (2): 60–63. doi:10.1016/j.tig.2008.11.003. PMID 19081651. edit

[3] ttp://www.tokyofoundation.org/en/series/japanese-traditional-foods/vol.-10-koji-an-aspergillus

[4] Shurtleff, W.; Aoyagi, A. History of Koji - Grains and/or Soybeans Enrobed with a Mold Culture (300 BCE to 2012). Lafayette, California: Soyinfo Center. 660 pp. (1,560 references; 142 photos and illustrations, Free online)

[MBKM-5] Kitamoto, Katsuhiko (2002). "Molecular Biology of the Koji Molds". Advances in Applied Microbiology. Advances in Applied Microbiology 51: 129–153. doi:10.1016/S0065-2164(02)51004-2. ISBN 9780120026531. PMID 12236056. Retrieved 2008-01-03.

[nobori-6] "In-depth". Retrieved 2007-01-24. (Japanese)

[nymtc-7] "What is Shochu?". Retrieved 2007-01-24.

[sakesake6-8] "Other terminology relating to Shochu and Awamori". Retrieved 2007-01-27. (Japanese)

[shochucircle-9] "Shochu Circle". Retrieved 2007-12-11.

[10] Goffeau, André (December 2005). "Multiple moulds". Nature 438 (7071): 1092–1093. doi:10.1038/4381092b. PMID 16371993.

[11] Machida, Masayuki et al. (December 2005). "Genome sequencing and analysis of Aspergillus oryzae". Nature 438 (7071): 1157–1161. doi:10.1038/nature04300. PMID 16372010.

[12] Galagan, James E. et al. (December 2005). "Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae". Nature 438 (7071): 1105–1115. doi:10.1038/nature04341. PMID 16372000.

[Wang-13] Wang, H.; Liu, L.; Guo, Y. -X.; Dong, Y. -S.; Zhang, D. -J.; Xiu, Z. -L. (2007). "Biotransformation of piceid in Polygonum cuspidatum to resveratrol by Aspergillus oryzae". Applied Microbiology and Biotechnology 75 (4): 763–768. doi:10.1007/s00253-007-0874-3. PMID 17333175. edit

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