Fungal enzymes used in oriental food and beverage industries

Sakaguchi, Kinichirô; Takagi, Masamichi; Horiuchi, Hiroyuki; Gomi, Katsuya

doi:10.1007/978-94-011-2930-5_3

Cited by 41 publications

(21 citation statements)

References 132 publications

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“…7A). Northern blot analysis showed that transcriptional repression of ␣-amylase-encoding genes (amyA, amyB, and amyC) (25) and MAL cluster genes (malP and malT) (4) by glucose was relieved in the ΔcreB mutant, and this repression was partially recovered in the ΔcreB ΔcreD mutant (Fig. 7B).…”

Section: Improved ␣-Amylase Production By Cred Mutantmentioning

confidence: 99%

Improved α-Amylase Production by Dephosphorylation Mutation of CreD, an Arrestin-Like Protein Required for Glucose-Induced Endocytosis of Maltose Permease and Carbon Catabolite Derepression in Aspergillusoryzae

Tanaka

Hiramoto

Tada

et al. 2017

Appl Environ Microbiol

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Aspergillus oryzae produces copious amount of amylolytic enzymes, and MalP, a major maltose permease, is required for the expression of amylase-encoding genes. The expression of these genes is strongly repressed by carbon catabolite repression (CCR) in the presence of glucose. MalP is transported from the plasma membrane to the vacuole by endocytosis, which requires the homolog of E6-AP carboxyl terminus ubiquitin ligase HulA, an ortholog of yeast Rsp5. In yeast, arrestin-like proteins mediate endocytosis as adaptors of Rsp5 and transporters. In the present study, we examined the involvement of CreD, an arrestin-like protein, in glucoseinduced MalP endocytosis and CCR of amylase-encoding genes. Deletion of creD inhibited the glucose-induced endocytosis of MalP, and CreD showed physical interaction with HulA. Phosphorylation of CreD was detected by Western blotting, and two serine residues were determined as the putative phosphorylation sites. However, the phosphorylation state of the serine residues did not regulate MalP endocytosis and its interaction with HulA. Although ␣-amylase production was significantly repressed by creD deletion, both phosphorylation and dephosphorylation mimics of CreD had a negligible effect on ␣-amylase activity. Interestingly, dephosphorylation of CreD was required for CCR relief of amylase genes that was triggered by disruption of the deubiquitinating enzyme-encoding gene creB. The ␣-amylase activity of the creB mutant was 1.6-fold higher than that of the wild type, and the dephosphorylation mimic of CreD further improved the ␣-amylase activity by 2.6-fold. These results indicate that a combination of the dephosphorylation mutation of CreD and creB disruption increased the production of amylolytic enzymes in A. oryzae. IMPORTANCEIn eukaryotes, glucose induces carbon catabolite repression (CCR) and proteolytic degradation of plasma membrane transporters via endocytosis. Glucoseinduced endocytosis of transporters is mediated by their ubiquitination, and arrestinlike proteins act as adaptors of transporters and ubiquitin ligases. In this study, we showed that CreD, an arrestin-like protein, is involved in glucose-induced endocytosis of maltose permease and carbon catabolite derepression of amylase gene expression in Aspergillus oryzae. Dephosphorylation of CreD was required for CCR relief triggered by the disruption of creB, which encodes a deubiquitinating enzyme; a combination of the phosphorylation-defective mutation of CreD and creB disruption dramatically improved ␣-amylase production. This study shows the dual function of an arrestin-like protein and provides a novel approach for improving the production of amylolytic enzymes in A. oryzae.

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Section: Improved ␣-Amylase Production By Cred Mutantmentioning

confidence: 99%

Improved α-Amylase Production by Dephosphorylation Mutation of CreD, an Arrestin-Like Protein Required for Glucose-Induced Endocytosis of Maltose Permease and Carbon Catabolite Derepression in Aspergillusoryzae

Tanaka

Hiramoto

Tada

et al. 2017

Appl Environ Microbiol

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“…It is well known that A. oryzae has three a-amylase genes (takaamylase genes: amyA, amyB and amyC) 13 that have almost identical nucleotide sequences with only one and two mismatches in the 5 0 -flanking and coding regions, respectively. The amyA gene has a transposon-like element at its 5 0 -flanking region, and the amyB and amyC genes have highly similar nucleotide sequences spanning approximately 5 kilobases (kb), including an incomplete transposon sequence at their 5 0 -flanking region.…”

Section: Superfamily (Mfs) Transporter Genes (Supplementarymentioning

confidence: 99%

Genome sequencing and analysis of Aspergillus oryzae

Machida

Asai²,

Sano

et al. 2005

Nature

1,113

710

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“…A. oryzae generally has multiple genes encoding Taka-amylase A, the number of which is two or three, depending on the strain. 22) In addition, two kinds of glucoamylase-encoding genes have so far been cloned from A. oryzae; one gene (glaA) 23) is highly homologous to the A. niger (A. awamori) glaA gene 24,25) and is expressed both in submerged and solid-state culture, and the other (glaB) 26) is also similar to the A. niger glaA, except for the absence of a starch-binding domain in the C-terminus, and the fact that it is expressed specifically in solid-state culture. One of three Taka-amylase genes (amyA) and the -glucosidase-encoding gene (agdA) 27) are clustered with their transcriptional activator gene (amyR) in the A. oryzae genome.…”

Section: Glycolytic Enzymesmentioning

confidence: 99%