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  1. Article: Role of two alpha-L-arabinofuranosidases in arabinoxylan degradation and characteristics of the encoding genes from shochu koji molds, Aspergillus kawachii and Aspergillus awamori.

    Koseki, Takuya / Okuda, Masaki / Sudoh, Shigetoshi / Kizaki, Yasuzo / Iwano, Kimio / Aramaki, Isao / Matsuzawa, Hiroshi

    Journal of bioscience and bioengineering

    2005  Volume 96, Issue 3, Page(s) 232–241

    Abstract: Two different alpha-L-arabinofuranosidases from Aspergillus kawachii were purified and characterized. The two enzymes acted synergically with xylanase in the degradation of arabinoxylan and resulted in an increase in the amount of ferulic acid release by ...

    Abstract Two different alpha-L-arabinofuranosidases from Aspergillus kawachii were purified and characterized. The two enzymes acted synergically with xylanase in the degradation of arabinoxylan and resulted in an increase in the amount of ferulic acid release by feruloyl esterase. Both enzymes were acidophilic and acid stable enzymes which had an optimum pH of 4.0 and were stable at pH 3.0-7.0. The general properties of the enzymes including pH optima and pH stability were similar to those of Aspergillus awamori. These results suggest that the alpha-L-arabinofuranosidases contribute to an increase in cereal utilization and formation of aroma in shochu brewing. Two different genes encoding alpha-L-arabinofuranosidases from A. kawachii, designated as AkabfA and AkabjB, and those from A. awamori, designated as AwabfA and AwabjB, were also cloned and characterized. The difference between the sequences of AkabfA and AwabfA was only one nucleotide, resulting in an amino acid difference in the sequence, and the enzymes were assigned to family 51 of glycoside hydrolases. On the other hand, the differences between the sequences of AkabjB and AwabjB and between their encoding proteins were two nucleotides and one amino acid residue, respectively, and the enzymes were assigned to family 54 of glycoside hydrolases. On comparison of the abfA and abjB genes among A. kawachii, A. awamori, and A. niger, the relationship between the two genes for A. kawachii and A. awamori was much closer than those between A. niger and the others. Northern analyses showed that transcription of AkabfB was greater than that of AkabfA in the presence of L-arabitol and L-arabinose, and that transcriptions of both genes were not induced in the presence of sucrose and glucose.
    Language English
    Publishing date 2005-10-03
    Publishing country Japan
    Document type Journal Article
    ZDB-ID 1465387-4
    ISSN 1347-4421 ; 1389-1723
    ISSN (online) 1347-4421
    ISSN 1389-1723
    DOI 10.1016/s1389-1723(03)80187-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Production of two types of phytase from Aspergillus oryzae during industrial koji making.

    Fujita, Jin / Shigeta, Seiko / Yamane, Yu-Ichi / Fukuda, Hisashi / Kizaki, Yasuzo / Wakabayashi, Saburo / Ono, Kazuhisa

    Journal of bioscience and bioengineering

    2005  Volume 95, Issue 5, Page(s) 460–465

    Abstract: In our previous study, it was determined that phytase produced by Aspergillus oryzae plays an important role in supplying phosphate to yeast in the process of making sake. During koji making, two types of phytase (Phy-I and Phy-II) are produced. The ... ...

    Abstract In our previous study, it was determined that phytase produced by Aspergillus oryzae plays an important role in supplying phosphate to yeast in the process of making sake. During koji making, two types of phytase (Phy-I and Phy-II) are produced. The purified phytases have high thermal and pH stability, in comparison to phytase purified from a submerged culture (ACP-II). In the present study, Phy-I and Phy-II retained their activities for 45 h. The NH2-terminal sequence of Phy-1, which is eight amino acids in length, was identical to that of ACP-II, but the molecular weights of these two forms, as estimated by SDS-PAGE, were quite different from each other (Phy-I, 120 kDa; ACP-II, 58 kDa). From the NH2-terminal amino acid sequence analysis of the predominant phytase (Phy-II), a molecular weight of 116 kDa was expected to reflect a new type of phytase produced only in koji culture. The substrate specificity of Phy-II was sufficiently broad that it hydrolyzed not only phytic acid and p-nitro phenyl phosphate, but also glucose 6-phosphate and glycerol 1-phosphate. In the process of making koji, Phy-I was produced at an early stage, followed by Phy-II; with both phytases being thought to function to hydrolyze phytic acid cooperatively.
    Language English
    Publishing date 2005-10-03
    Publishing country Japan
    Document type Journal Article
    ZDB-ID 1465387-4
    ISSN 1347-4421 ; 1389-1723
    ISSN (online) 1347-4421
    ISSN 1389-1723
    DOI 10.1016/s1389-1723(03)80045-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Production and properties of phytase and acid phosphatase from a sake koji mold, Aspergillus oryzae.

    Fujita, Jin / Yamane, Yu-Ichi / Fukuda, Hisashi / Kizaki, Yasuzo / Wakabayashi, Saburo / Shigeta, Seiko / Suzuki, Osamu / Ono, Kazuhisa

    Journal of bioscience and bioengineering

    2005  Volume 95, Issue 4, Page(s) 348–353

    Abstract: We identified three types of acid phosphatase (ACP-I, ACP-II, and ACP-III) produced by Aspergillus oryzae in a submerged culture using only phytic acid as the phosphorous substrate. The optimum pH for the activities of the three enzymes was in the range ... ...

    Abstract We identified three types of acid phosphatase (ACP-I, ACP-II, and ACP-III) produced by Aspergillus oryzae in a submerged culture using only phytic acid as the phosphorous substrate. The optimum pH for the activities of the three enzymes was in the range of 4.5 to 5.5. Analysis of the substrate specificities of these enzymes revealed that ACP-I and ACP-III were acid phosphatases, and ACP-II was a phytase. These enzymes were produced during different periods of mycelial growth: ACP-II was produced during the early phase of cultivation (around 24 h), and ACP-I was produced between 24 to 72 h. ACP-III was detected after the production of ACP-I and ACP-II had ceased. The release of phosphate from phytic acid was expected to be due to the cooperative hydrolysis of these enzymes.
    Language English
    Publishing date 2005-10-03
    Publishing country Japan
    Document type Journal Article
    ZDB-ID 1465387-4
    ISSN 1347-4421 ; 1389-1723
    ISSN (online) 1347-4421
    ISSN 1389-1723
    DOI 10.1016/s1389-1723(03)80066-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Production of cellulose- and xylan-degrading enzymes by a koji mold, aspergillus oryzae, and their contribution to the maceration of rice endosperm cell wall.

    Yamane, Yu-Ichi / Fujita, Jin / Shimizu, Ryu-Ichi / Hiyoshi, Akira / Fukuda, Hisashi / Kizaki, Yasuzo / Wakabayashi, Saburo

    Journal of bioscience and bioengineering

    2002  Volume 93, Issue 1, Page(s) 9–14

    Abstract: The production of cellulose- (CEL), xylan- (XYL), and pectin-degrading enzymes (PEC) by a koji mold, Aspergillus oryzae, was studied, and their contributions to the maceration of the rice endosperm cell wall were investigated with regard to the ... ...

    Abstract The production of cellulose- (CEL), xylan- (XYL), and pectin-degrading enzymes (PEC) by a koji mold, Aspergillus oryzae, was studied, and their contributions to the maceration of the rice endosperm cell wall were investigated with regard to the utilization of available rice in the sake mash. The sake koji mold showed higher CEL and XYL productivities, whereas the miso and soy sauce koji molds showed higher PEC productivity. Statistical analyses indicated that CEL and XYL contribute predominantly and synergistically to the maceration of the rice endosperm cell wall. A. oryzae produced at least three kinds of CEL (Cel-1, 2, 3) and two kinds of XYL (Xyl-1, 2) when cultured in a wheat bran medium. In the solid-state culture, the production of Cel-3 and Xyl-2 was markedly stimulated by decreasing the moisture content of the solid substrate, although the production levels of Cel-1 and Xyl-1 were almost the same. These data suggest that the production of Cel-3 and Xyl-2 is strongly influenced by culture conditions, and that water activity is one of the dominant factors in the regulation of their production.
    Language English
    Publishing date 2002
    Publishing country Japan
    Document type Journal Article
    ZDB-ID 1465387-4
    ISSN 1347-4421 ; 1389-1723
    ISSN (online) 1347-4421
    ISSN 1389-1723
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Properties of cellulose-degrading enzymes from Aspergillus oryzae and their contribution to material utilization and alcohol yield in sake mash fermentation.

    Yamane, Yu-Ichi / Fujita, Jin / Izuwa, Shinya / Fukuchi, Kaoru / Shimizu, Ryu-Ichi / Hiyoshi, Akira / Fukuda, Hisashi / Mikami, Shigeaki / Kizaki, Yasuzo / Wakabayashi, Saburo

    Journal of bioscience and bioengineering

    2005  Volume 93, Issue 5, Page(s) 479–484

    Abstract: Four cellulose-degrading enzymes were identified in a solid-state culture of Aspergillus oryzae. The three major enzymes were purified and named Cel-1, Cel-2, and Cel-3, respectively. The molecular weights were determined to be 62, 120, and 34 kDa, ... ...

    Abstract Four cellulose-degrading enzymes were identified in a solid-state culture of Aspergillus oryzae. The three major enzymes were purified and named Cel-1, Cel-2, and Cel-3, respectively. The molecular weights were determined to be 62, 120, and 34 kDa, respectively. The optimum temperature of Cel-3 activity was higher than that of the other enzymes. An acidic pH was found to be more suitable for Cel-1 activity than for the other enzymes, and Cel-3 was more stable under acidic conditions than the other two. These properties and the results of a protein homology search for N-terminal amino acid sequences suggest that Cel-1 and Cel-3 correspond to the previously isolated endo-1,4-beta-glucanase CelB and CelA, respectively. The analysis of substrate specificity suggested that Cel-2 is likely to be beta-glucosidase. The effect of Cel-1, Cel-2, and Cel-3 on the sake mash fermentation was determined and it was found that Cel-2 markedly improved material utilization and alcohol yield in sake mash fermentation.
    Language English
    Publishing date 2005-10-03
    Publishing country Japan
    Document type Journal Article
    ZDB-ID 1465387-4
    ISSN 1347-4421 ; 1389-1723
    ISSN (online) 1347-4421
    ISSN 1389-1723
    DOI 10.1016/s1389-1723(02)80095-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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