Shinichi Ohashi
Kanazawa Institute of Technology
23 Papers
128 Citations
Shinichi Ohashi is an academic researcher from Kanazawa Institute of Technology. The author has contributed to research in topics: Aspergillus oryzae & Kojic acid. The author has an hindex of 10, co-authored 23 publications.
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Papers
Kojic acid biosynthesis in Aspergillus oryzae is regulated by a Zn(II)(2)Cys(6) transcriptional activator and induced by kojic acid at the transcriptional level.
Junichiro Marui,Noriko Yamane,Sumiko Ohashi-Kunihiro,Tomohiro Ando,Yasunobu Terabayashi,Motoaki Sano,Shinichi Ohashi,Eiji Ohshima,Kuniharu Tachibana,Yoshitaka Higa,Marie Nishimura,Hideaki Koike,Masayuki Machida,Masayuki Machida +13 more
TL;DR: A gene encoding the Zn(II)(2)Cys(6) transcriptional factor was determined to be essential for KA production and the transcriptional activation of KA biosynthetic genes, which were triggered by the addition to Aspergillus oryzae.
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The Glucoamylase-Encoding Gene (glaB) Is Expressed in Solid-State Culture with A Low Water Content
TL;DR: Using the real-time quantitative reverse transcriptase-polymerase chain reaction, it is confirmed that expression of the glucoamylase-encoding gene in A. oryzae cultured in solid-state culture depends on the water content of the culture.
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Regio- and Stereoselective Subterminal Hydroxylations of n -Decane by Fungi in a Liquid–Liquid Interface Bioreactor (L–L IBR)
TL;DR: This article may be the first report to describe the excellent regio- and stereoselective subterminal hydroxylations of n-alkane with microorganisms.
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Synthesis of (−)-β-caryophyllene oxide via regio- and stereoselective endocyclic epoxidation of β-caryophyllene with Nemania aenea SF 10099-1 in a liquid–liquid interface bioreactor (L–L IBR)
TL;DR: Although the strain could not grow below pH 5.5, the endocyclic epoxidation of Car efficiently proceeded at a wide range of initial medium pH (6.0 to 9.0), and the bioconversion system exhibited an excellent alleviation effect toward substrate and product inhibitions.
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Purification and characterization of β-Mannanase from Reinekea sp. KIT-YO10 with transglycosylation activity
TL;DR: β-Mannanase from the strain KIT YO10 possessed transglycosylation activity for mannooligosaccharides and was thermostable and thermophile compared to the β-mannanase of other marine bacteria.
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