Production and properties of phytase and acid phosphatase from a sake koji mold, Aspergillus oryzae

Fujita, Jin; Yamane, Yuko; Fukuda, Hisashi; Kizaki, Yasuzo; Wakabayashi, Saburo; Shigeta, Seiko; Сузукі, Осаму; Ono, Kazuhisa

doi:10.1016/s1389-1723(03)80066-x

Cited by 30 publications

(32 citation statements)

References 17 publications

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“…AphA was stable up to 35℃ and inactivated sharply at temperatures above 35℃. As shown in Table 3, the temperature optimum and thermal stability of AphA were similar to those of A. oryzae ACP-II, while the pH optimum and pH stability of AphA were different from those of A. oryzae ACP-II (Fujita et al, 2003a). On the other hand, the pH and temperature optima for AphA were lower than reported for the identical gene products overexpressed in another A. oryzae strain previously reported (Uchida et al, 2006).…”

Section: Resultssupporting

confidence: 52%

“…As shown in Table 4, AphA had a different substrate specificity that that of other A. oryzae acid phosphatases. On the basis of the differences in the N-terminal amino acid sequence, enzymatic features, and substrate specificity, AphA is distinct from the acid phosphates or phytases reported by Fujita et al (2003aFujita et al ( , 2003b and Shimizu (1993).…”

Section: Resultsmentioning

confidence: 80%

“…Although some of them have been purified and their N-terminal amino acid sequences determined (Fujita et al, 2003a(Fujita et al, , 2003b, the corresponding genes encoding them could not be found in the genome database of A. oryzae (i). Therefore, we surveyed putative acid phosphatase genes from the A. oryzae genome database by BLAST search.…”

Section: Resultsmentioning

confidence: 99%

“…c ND, not determined. The results of ACP-I, ACP-II and ACP-III were taken from the report by Fujita et al (2003a). c The results of AphK1 were taken from the report by Shimizu (1993).…”

Section: Resultsmentioning

confidence: 99%

“…Although several studies on acid phosphatases and phytases from A. oryzae have been reported (Fujishima et al, 1966;Wang et al, 1980;Oike et al, 1984;Shimizu, 1993;Fujita et al, 2003aFujita et al, , 2003b, little is yet known about their dephosphorylation activity on disodium 5'-ribonucleotides. Phytases belong to the family of histidine acid phosphatases, a subclass of phosphatases.…”

Section: Introductionmentioning

confidence: 99%

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Disruption and Overexpression of Acid Phosphatase Gene (aphA) from a Miso Koji Mold, Aspergillus oryzae KBN630, and Characterization of the Gene Product

Yoshino-Yasuda

Hasegawa

Iga³

et al. 2012

FSTR

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An acid phosphatase gene (aphA gene) from an industrial miso koji mold strain, A. oryzae KBN630, was disrupted by using the recently developed homologous gene replacement system for this strain. The aphA gene disruption did not affect growth on steamed soybean. Acid phosphatase production decreased by approximately 20% in the aphA gene disruptants compared with that of the wild-type strain. Utilizing the promoter of the A. oryzae TEF1 gene, AphA expressed in A. oryzae was successfully secreted into the culture medium. AphA had a molecular mass of 58.0 to 65.0 kDa, a pH optimum of 4.0, and a temperature optimum of 40℃. AphA had the ability to release inorganic phosphate from GMP and IMP. This is the first report to show directly that an A. oryzae acid phosphatase has the ability to hydrolyze GMP and IMP.

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Section: Resultssupporting

confidence: 52%

Section: Resultsmentioning

confidence: 80%

Section: Resultsmentioning

confidence: 99%

“…c ND, not determined. The results of ACP-I, ACP-II and ACP-III were taken from the report by Fujita et al (2003a). c The results of AphK1 were taken from the report by Shimizu (1993).…”

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Disruption and Overexpression of Acid Phosphatase Gene (aphA) from a Miso Koji Mold, Aspergillus oryzae KBN630, and Characterization of the Gene Product

Yoshino-Yasuda

Hasegawa

Iga³

et al. 2012

FSTR

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Ferulic Acid Production in the Brewing of Rice Wine (Sake)

Uno

Itoh

Miyamoto³

et al. 2009

Journal of the Institute of Brewing

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The traditional Japanese alcoholic beverage sake is produced by fermentation of rice by Saccharomyces cerevisiae and Aspergillus oryzae. A. oryzae releases ferulic acid, an antioxidant, from steamed rice during the fermentation process. The concentration of ferulic acid increased with time during fermentation and the production rate peaked 9-12 days post inoculation. Analysis of the fermentation cultures of Aspergillus oryzae, by highperformance liquid chromatography (HPLC), revealed that pcoumaric acid induced an 18.9-fold increase in the level of ferulic acid. Furthermore, SDS-PAGE analysis revealed an increase or decrease in the level of specific proteins after the addition of p-coumaric acid to fermentation cultures of Aspergillus oryzae. Ferulate esterase (FAE) activity was observed in the fermented sake ten days following the start of the fermentation process. These results suggest that the level of ferulic acid is regulated by the enzymes synthesized by A. oryzae during the sake brewing process.

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Ferulic Acid Release and 4-Vinylguaiacol Formation during Chinese Rice Wine Brewing and Fermentation

2010

Journal of the Institute of Brewing

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J. Inst. Brew. 116(3), 304-311, 2010The release of ferulic acid (FA) and the subsequent enzymatic decarboxylation to 4-vinylguaiacol (4-VG) were nearly ubiquitous during the production of Chinese rice wine. To evaluate the release of FA and the transformation to 4-VG, the levels of FA and 4-VG were determined by high performance liquid chromatography (HPLC) and gas chromatography-mass spectrum (GC-MS), respectively. During rice wine brewing, the concentrations of FA and 4-VG increased as fermentation time prolonged, with a rapid rise in days 1 to 5 of the main fermentation and followed by a slower rise from the 6th day post inoculation. FA and 4-VG levels in mashes, fermented by yeast with wheat Qu, were significantly higher than those in mashes fermented by yeast using commercial enzyme additions. The release of FA from rice by wheat Qu involves an enzymatic release mechanism. The levels of FA and 4-VG from rice flour by wheat Qu rose gradually during the first 24 h and then tended to stabilize. The capacity of yeasts to decarboxylate phenolic acids (Pof + phenotype) was absent in most rice wine brewing yeasts. These results suggest that the production of FA and 4-VG originated from materials in the wheat Qu rather than by the yeast during Chinese rice wine brewing and fermentation.

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Production and properties of phytase and acid phosphatase from a sake koji mold, Aspergillus oryzae

Cited by 30 publications

References 17 publications

Disruption and Overexpression of Acid Phosphatase Gene (aphA) from a Miso Koji Mold, Aspergillus oryzae KBN630, and Characterization of the Gene Product

Disruption and Overexpression of Acid Phosphatase Gene (aphA) from a Miso Koji Mold, Aspergillus oryzae KBN630, and Characterization of the Gene Product

Ferulic Acid Production in the Brewing of Rice Wine (Sake)

Ferulic Acid Release and 4-Vinylguaiacol Formation during Chinese Rice Wine Brewing and Fermentation

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