Binding of α-amylase to the cell wall of Aspergillus oryzae

Tonomura, Kenzo; Futai, Fusae; Takahashi, Osamu

doi:10.1016/0006-3002(63)91068-0

Cited by 7 publications

(1 citation statement)

References 8 publications

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“…Historically, α-amylase, also known as Taka-amylase A from Takadiastase, was isolated and crystallized from A. oryzae cultures in the 1950s [ 10 , 11 ]. The enzymatic activity of α-amylase was found in both the culture medium and mycelium, suggesting that α-amylase is not only secreted to the medium but also localized to the cell surface [ 12 ]. Indeed, localization analysis by an indirect fluorescent-antibody technique using the antiserum against α-amylase demonstrated that α-amylase is located on the cell surface [ 13 ].…”

Section: Secretory Pathwaymentioning

confidence: 99%

Membrane Traffic in Aspergillus oryzae and Related Filamentous Fungi

Higuchi

2021

JoF

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The industrially important filamentous fungus Aspergillus oryzae, known as the yellow Koji mold and also designated the Japanese National fungus, has been investigated for understanding the intracellular membrane trafficking machinery due to the great ability of valuable enzyme production. The underlying molecular mechanisms of the secretory pathway delineate the main secretion route from the hyphal tip via the vesicle cluster Spitzenkörper, but also there is a growing body of evidence that septum-directed and unconventional secretion occurs in A. oryzae hyphal cells. Moreover, not only the secretory pathway but also the endocytic pathway is crucial for protein secretion, especially having a role in apical endocytic recycling. As a hallmark of multicellular filamentous fungal cells, endocytic organelles early endosome and vacuole are quite dynamic: the former exhibits constant long-range motility through the hyphal cells and the latter displays pleiomorphic structures in each hyphal region. These characteristics are thought to have physiological roles, such as supporting protein secretion and transporting nutrients. This review summarizes molecular and physiological mechanisms of membrane traffic, i.e., secretory and endocytic pathways, in A. oryzae and related filamentous fungi and describes the further potential for industrial applications.

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Section: Secretory Pathwaymentioning

confidence: 99%

Membrane Traffic in Aspergillus oryzae and Related Filamentous Fungi

Higuchi

2021

JoF

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Aminoacylase pellets

Hirano

Karube

Suzuki

1977

Biotech & Bioengineering

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Aminoacylase was immobilized on the mycelium pellets of Aspergillus ochraceus by using albumin and glutaraldehyde. No difference in the optimum pH was observed between native aminoacylase and aminoacylase pellets. The aminoacylase pellets were stable in pH 4-8 but they were unstable in alkaline conditions. The aminoacylase pellets were more stable against heavy metal ions and inhibitors than native aminoacylase. However, the degree of the activation of aminoacylase with cobalt ion decreased with the immobilization. It was suggested that most of aminoacylase was covalently coupled to the mycelium with glutaraldehyde.

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