Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Noribumi, Tomiyama"'
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 66:262-270
The sldA gene that encodes the D-sorbitol dehydrogenase (SLDH) from Gluconobacter suboxydans IFO 3255 was cloned and sequenced. It encodes a polypeptide of 740 residues, which contains a signal sequence of 24 residues. SLDH had 35–37% identity to t
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 66:2314-2322
The D-sorbitol dehydrogenase gene, sldA, and an upstream gene, sldB, encoding a hydrophobic polypeptide, SldB, of Gluconobacter suboxydans IFO 3255 were disrupted in a check of their biological functions. The bacterial cells with the sldA gene disrup
Publikováno v:
Biochimica et biophysica acta. 1647(1-2)
Gluconobacter strains effectively produce l -sorbose from d -sorbitol because of strong activity of the d -sorbitol dehydrogenase (SLDH). l -sorbose is one of the important intermediates in the industrial vitamin C production process. Two kinds of me
Autor:
Yoshikazu Fujii, Hirohide Toyama, Taro Miyazaki, Masako Shinjoh, Osao Adachi, Noribumi Tomiyama, Yoshitaka Ano, Tatsuo Hoshino, Kazunobu Matsushita, Teruhide Sugisawa
Acetic acid bacteria, especially Gluconobacter species, have been known to catalyze the extensive oxidation of sugar alcohols (polyols) such as d -mannitol, glycerol, d -sorbitol, and so on. Gluconobacter species also oxidize sugars and sugar acids a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a342264f0c150929b4951af6dec7a928
https://europepmc.org/articles/PMC154820/
https://europepmc.org/articles/PMC154820/
Publikováno v:
Bioscience, biotechnology, and biochemistry. 66(2)
The sldA gene that encodes the D-sorbitol dehydrogenase (SLDH) from Gluconobacter suboxydans IFO 3255 was cloned and sequenced. It encodes a polypeptide of 740 residues, which contains a signal sequence of 24 residues. SLDH had 35-37% identity to the
Publikováno v:
Applied and environmental microbiology. 61(5)
Cloning and expression of the gene encoding Acetobacter liquefaciens IFO 12258 membrane-bound L-sorbosone dehydrogenase (SNDH) were studied. A genomic library of A. liquefaciens IFO 12258 was constructed with the mobilizable cosmid vector pVK102 (mob
Publikováno v:
FEBS Letters. 181:143-148
The differences in the outer membrane permeation between two major subgroups of β-lactam antibiotics were studied. The permeation of cephalosporins was closely related to porin channels in the outer membrane. In contrast, the outer membrane permeati
Publikováno v:
FEBS letters. 208(1)
Both Mg2+ and Na+ stimulated the outer membrane permeation of negatively charged cephalosporins in Escherichia coli without any significant alteration of the permeation of a zwitterionic cephalosporin. Such stimulation was not observed in an E. coli