Lethal and mutagenic effects of ion beams and γ-rays in Aspergillus oryzae.

Aspergillus oryzae is a fungus that is used widely in traditional Japanese fermentation industries. In this study, the lethal and mutagenic effects of different linear energy transfer (LET) radiation in freeze-dried conidia of A. oryzae were investigated.

Development of a new single-bottle multi-purpose primer for bonding to dental porcelain, alumina, zirconia, and dental gold alloy.

This study investigated the bonding efficacy of a combined primer application which comprised a silane coupling agent, an acidic adhesive monomer, and a dithiooctanoate monomer, as well as the influence of shelf life on bonding. Five experimental primers (coded as Si-P-SS-1 to Si-P-SS-4, and Si-SS as the control) were prepared using 20.0-40.

Design of a new, multi-purpose, light-curing adhesive comprising a silane coupling agent, acidic adhesive monomers and dithiooctanoate monomers for bonding to varied metal and dental ceramic materials.

A newly designed, light-curing adhesive was investigated for its bonding effectiveness to porcelain, alumina, zirconia, Au, Au alloy, Ag alloy, Au-Ag-Pd alloy, and Ni-Cr alloy. Four experimental adhesives were prepared using varying contents of the following: a silane coupling agent [3-methacryloyloxypropyltriethoxysilane (3-MPTES)], acidic adhesive monomers [6-methacryloyloxyhexyl phosphonoacetate(6-MHPA),6-methacryloyloxyhexyl3-phosphonopropionate(6-MHPP)and 4-methacryloyloxyethoxycarbonylphthalic acid (4-MET)], and dithiooctanoate monomers [6-methacryloyloxyhexyl 6,8-dithiooctanoate (6-MHDT) and 10-methacryloyloxydecyl 6,8-dithiooctanoate (10-MDDT)]. After all adherend surfaces were sandblasted and applied with an experimental adhesive, shear bond strengths (SBSs) of a light-curing resin composite (Beautifil II, Shofu Inc.

Xylose triggers reversible phosphorylation of XlnR, the fungal transcriptional activator of xylanolytic and cellulolytic genes in Aspergillus oryzae.

XlnR is a transcription factor that mediates D-xylose-triggered induction of xylanolytic and cellulolytic genes in Aspergillus. In order to clarify the molecular mechanisms underlying XlnR-mediated induction, Aspergillus oryzae XlnR was fused with the c-myc tag and examined by Western blotting. Phosphate-affinity SDS-PAGE revealed that XlnR was present as a mixture of variously phosphorylated forms in the absence of D-xylose, and that D-xylose triggered additional phosphorylation of the protein.

Loss of Aspergillus oryzae amyR function indirectly affects hemicellulolytic and cellulolytic enzyme production.

Aspergillus oryzae AB390, a derivative of A. oryzae OR101, was found to be suitable for soy sauce production, yielding a product light brown in color. Compared to the parent strain, hemicellulase and cellulase activities in the mutant were higher; however, its amylase activity was found to be much lower.

Characterization of Aspergillus oryzae aspartyl aminopeptidase expressed in Escherichia coli.

To characterize aspartyl aminopeptidase from Aspergillus oryzae, the recombinant enzyme was expressed in Escherichia coli. The enzyme cleaves N-terminal acidic amino acids. About 30% activity was retained in 20% NaCl.