Cloning and Nucleotide Sequence of the Acid Protease-encoding Gene (<i>pepA</i>) from<i>Aspergillus oryzae</i>

Gomi, Katsuya; Arikawa, Kenji; Kamiya, Naokata; Kitamoto, Katsuhiko; Kumagai, Chieko

doi:10.1271/bbb.57.1095

Cited by 61 publications

(24 citation statements)

References 9 publications

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“…A. oryzae has 12 cysteine endopetidase genes, but no papain-like cysteine endopeptidase gene is present, confirming the previous suggestion that Aspergillus species do not produce papain-like enzymes to the culture broth. Although only four aspartic endopeptidase (EC 3.4.23.18) genes [38][39][40] and one serine-type carboxypeptidase (EC 3.4.16.-) gene 41) have been cloned and sequenced to date, there are 12 serine-type carboxypeptidase genes and 11 aspartic endopeptidase genes in the A. oryzae genome. Among these, seven serine-type carboxypeptidase genes and eight aspartic endopeptidase genes are present in the EST data base of A. oryzae.…”

Section: Proteolytic Enzymesmentioning

confidence: 99%

Genomics ofAspergillus oryzae

Kobayashi

Abe

Asai

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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171

118

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Section: Proteolytic Enzymesmentioning

confidence: 99%

Genomics ofAspergillus oryzae

Kobayashi

Abe

Asai

et al. 2007

Bioscience, Biotechnology, and Biochemistry

Self Cite

171

118

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“…Fungal proteinases have been investigated in saprophytes with industrial applications, like certain aspergilli (Gomi et al, 1993;Jarai et al, 1994a) and penicilli (James & Sielecki, 1983;Durand-Poussereau & Fevre, 1996), but also in fungal pathogens that cause human disease, such as Candida spp. (Hube, 1998;Monod et al, 1993), Rhizopus spp.…”

Section: B Cinerea Cultures Exclusively Contain Secreted Ap Activitymentioning

confidence: 99%

An aspartic proteinase gene family in the filamentous fungus Botrytis cinerea contains members with novel features

et al. 2004

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Botrytis cinerea, an important fungal plant pathogen, secretes aspartic proteinase (AP) activity in axenic cultures. No cysteine, serine or metalloproteinase activity could be detected. Proteinase activity was higher in culture medium containing BSA or wheat germ extract, as compared to minimal medium. A proportion of the enzyme activity remained in the extracellular glucan sheath. AP was also the only type of proteinase activity in fluid obtained from B. cinerea-infected tissue of apple, pepper, tomato and zucchini. Five B. cinerea genes encoding an AP were cloned and denoted Bcap1–5. Features of the encoded proteins are discussed. BcAP1, especially, has novel characteristics. A phylogenetic analysis was performed comprising sequences originating from different kingdoms. BcAP1 and BcAP5 did not cluster in a bootstrap-supported clade. BcAP2 clusters with vacuolar APs. BcAP3 and BcAP4 cluster with secreted APs in a clade that also contains glycosylphosphatidylinositol-anchored proteinases from Saccharomyces cerevisiae and Candida albicans. All five Bcap genes are expressed in liquid cultures. Transcript levels of Bcap1, Bcap2, Bcap3 and Bcap4 are subject to glucose and peptone repression. Transcripts from all five Bcap genes were detected in infected plant tissue, indicating that at least part of the AP activity in planta originates from the pathogen.

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“…Based on research with rice kernel solid-state fermentations (SSF) with Aspergillus oryzae, it was shown that high levels of glucoamylase B, an enzyme that is clearly different from glucoamylase A , are due mainly to induction of the glucoamylase B gene . Until now, gene expression studies have focussed only on transcriptional regulation of glaB ) and pepA (Gomi et al 1993) in surface-grown filamentous fungi like A. oryzae. Transcription levels of the acid protease-encoding gene (pepA) have been shown to decrease due to high temperatures (>38°C) when A. oryzae was cultured on rice kernels (Kitano et al 2002).…”

Section: Introductionmentioning

confidence: 99%

Different control mechanisms regulate glucoamylase and protease gene transcription in Aspergillus oryzae in solid-state and submerged fermentation

Biesebeke

Biezen

Vos

et al. 2004

Appl Microbiol Biotechnol

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Solid-state fermentation (SSF) with Aspergillus oryzae results in high levels of secreted protein. However, control mechanisms of gene expression in SSF have been only poorly studied. In this study we show that both glucoamylase (glaB) and protease (alpA, nptB) genes are highly expressed during surface cultivation on wheatbased solid medium, and even higher during cultivation on wheat kernels. In wheat-based liquid medium, low levels of gene expression are observed. Typical SSF cultivation conditions, such as low water activity and the formation of aerial hyphae, did not contribute to the high-level gene expression on wheat-based solid medium. Analysis of wheat-based solid and liquid cultivations showed differences in carbon and nitrogen utilisation and external pH. The results presented show that the difference in regulation of transcription of the alpA and nptB genes in wheatbased liquid and solid medium could be pH dependent, involving a pH-dependent transcription regulator. The results obtained suggest that the difference in regulation of transcription of the glaB gene in wheat-based liquid and solid medium is caused by a difference in carbohydrate degradation and consumption under the different culture conditions.

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Cloning and Nucleotide Sequence of the Acid Protease-encoding Gene (pepA) fromAspergillus oryzae

Cited by 61 publications

References 9 publications

Genomics ofAspergillus oryzae

Genomics ofAspergillus oryzae

An aspartic proteinase gene family in the filamentous fungus Botrytis cinerea contains members with novel features

Different control mechanisms regulate glucoamylase and protease gene transcription in Aspergillus oryzae in solid-state and submerged fermentation

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