Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Hidenobu Komeda"'
Publikováno v:
Biological Control. 124:53-60
The objectives of this study were to screen chitinase producing microorganisms to inhibit Rigidoporus microporus (white root rot) and to analyze the bioactive compounds produced by the selected strain using gas chromatography mass spectrometry (GC–
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ed38193358de67ee72b3dbb63c01c613
https://doi.org/10.1016/j.biocontrol.2018.01.007
https://doi.org/10.1016/j.biocontrol.2018.01.007
Publikováno v:
Journal of Bioscience and Bioengineering. 123:20-27
Meyerozyma caribbica strain 5XY2, which was isolated from an alcohol fermentation starter in Thailand, was found to catabolize l -arabinose as well as d -glucose and d -xylose. The highest production amounts of ethanol from d -glucose, xylitol from d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac8566a4e7b569b22b7ed6ca0554d419
https://doi.org/10.1016/j.jbiosc.2016.07.011
https://doi.org/10.1016/j.jbiosc.2016.07.011
Publikováno v:
Bioscience, biotechnology, and biochemistry. 81(8)
l-Xylulose reductase (LXR) catalyzes the reduction of l-xylulose to xylitol in the fungal l-arabinose catabolic pathway. LXR (RpLXR) was purified from the pentose-fermenting zygomycetous fungus Rhizomucor pusillus NBRC 4578. The native RpLXR is a hom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c4f35a30fc5e70a42d3fb9b36d795aa
https://pubmed.ncbi.nlm.nih.gov/28471330
https://pubmed.ncbi.nlm.nih.gov/28471330
l-Xylulose reductase (LXR) catalyzes the reduction of l-xylulose to xylitol in the fungal l-arabinose catabolic pathway. LXR (RpLXR) was purified from the pentose-fermenting zygomycetous fungus Rhizomucor pusillus NBRC 4578. The native RpLXR is a hom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41974666d8a4a6b818728d32fb69d347
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 78:1943-1953
The zygomycetous fungus Rhizomucor pusillus NBRC 4578 is able to ferment not only d-glucose but also d-xylose into ethanol. Xylitol dehydrogenase from R. pusillus NBRC 4578 (RpXDH), which catalyzes the second step of d-xylose metabolism, was purified
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbf6a83d64de6585c505edbf1123e24c
https://doi.org/10.1080/09168451.2014.943646
https://doi.org/10.1080/09168451.2014.943646
Characterization and application of aminoamide-oxidizing enzyme from Aspergillus carbonarius AIU 205
Publikováno v:
Journal of Bioscience and Bioengineering. 117:263-268
We isolated Aspergillus carbonarius AIU 205 as a new producer of an enzyme catalyzing oxidative deamination of 4-aminobutanamide (4-ABAD) to 4-oxobutanamide with the subsequent release of ammonia and hydrogen peroxide. Since the strain produced three
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77f977eb2f3527fb93e4f169e36a5f7f
https://doi.org/10.1016/j.jbiosc.2013.08.019
https://doi.org/10.1016/j.jbiosc.2013.08.019
Publikováno v:
Protein Engineering, Design and Selection. 24:607-616
Low protein solubility of recombinantly expressed proteins in Escherichia coli is a major factor hindering their application and analysis. We generated highly in vivo soluble mutants of a hydroxynitrile lyase in E.coli using protein engineering. Stru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52264e6f15a80211b1d578f84eb8e3a3
https://doi.org/10.1093/protein/gzr030
https://doi.org/10.1093/protein/gzr030
Autor:
Yasuyoshi Sakai, Hiroya Yurimoto, Yasuhisa Asano, Yasuhisa Fukuta, Samik Nanda, Yasuo Kato, Hidenobu Komeda
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 75:214-220
PmHNL, a hydroxynitrile lyase from Japanese apricot ume (Prunus mume) seed was purified to homogeneity by ammonium sulfate fractionation and chromatographic steps. The purified enzyme was a monomer with molecular mass of 58 kDa. It was a flavoprotein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6ad7b1cd99f793c8a02284fb20a6f2f
https://doi.org/10.1271/bbb.100187
https://doi.org/10.1271/bbb.100187
Publikováno v:
Enzyme and Microbial Technology. 46:237-245
Rhodococcus sp. strain Oct1 utilizing ω-octalactam as a sole source of carbon and nitrogen was isolated from soil. ω-Octalactam hydrolyzing enzyme was purified to homogeneity. The purified enzyme has a molecular weight of approximately 48,100 by SD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::675914c2dbdee3bba6ccdc45d10ea848
https://doi.org/10.1016/j.enzmictec.2009.09.010
https://doi.org/10.1016/j.enzmictec.2009.09.010
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 73:980-986
The genes encoding omega-laurolactam hydrolases from Cupriavidus sp. T7, Acidovorax sp. T31, Cupriavidus sp. U124, and Sphingomonas sp. U238 were cloned and sequenced. Nucleotide and amino acid sequence analysis of the four genes indicated that the p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef332b7fef52bfdb38654298f532442f
https://doi.org/10.1271/bbb.80551
https://doi.org/10.1271/bbb.80551