Hoshino A

References (2)

Title : Lateral transfer of the lux gene cluster - Kasai_2007_J.Biochem_141_231
Author(s) : Kasai S , Okada K , Hoshino A , Iida T , Honda T
Ref : J Biochem , 141 :231 , 2007
Abstract : The lux operon is an uncommon gene cluster. To find the pathway through which the operon has been transferred, we sequenced the operon and both flanking regions in four typical luminous species. In Vibrio cholerae NCIMB 41, a five-gene cluster, most genes of which were highly similar to orthologues present in Gram-positive bacteria, along with the lux operon, is inserted between VC1560 and VC1563, on chromosome 1. Because this entire five-gene cluster is present in Photorhabdus luminescens TT01, about 1.5 Mbp upstream of the operon, we deduced that the operon and the gene cluster were transferred from V. cholerae to an ancestor of Pr. luminescens. Because in both V. fischeri and Shewanella hanedai, luxR and luxI were found just upstream of the operon, we concluded that the operon was transferred from either species to the other. Because most of the genes flanking the operon were highly similar to orthologues present on chromosome 2 of vibrios, we speculated that the operon of most species is located on this chromosome. The undigested genomic DNAs of five luminous species were analysed by pulsed-field gel electrophoresis and Southern hybridization. In all the species except V. cholerae, the operons are located on chromosome 2.
ESTHER : Kasai_2007_J.Biochem_141_231
PubMedSearch : Kasai_2007_J.Biochem_141_231
PubMedID: 17169972
Gene_locus related to this paper: phopo-luxd , sheha-a0zsg8 , sheha-LUXD

Title : Degradation of aliphatic polyester films by commercially available lipases with special reference to rapid and complete degradation of poly(L-lactide) film by lipase PL derived from Alcaligenes sp - Hoshino_2002_Biodegradation_13_141
Author(s) : Hoshino A , Isono Y
Ref : Biodegradation , 13 :141 , 2002
Abstract : Commercial lipases were examined for their degradation efficiency of aliphatic polyester films. In 100 days immersion of polyester films in lipase solutions at 37 degrees C at pH 7.0, Lipase Asahi derived from Chromobacterium viscosum degraded polybutylene succinate-co-adipate (PBSA), poly (e-caprolactone) (PCL) and polybutylene succinate (PBS), and Lipase F derived from Rhizopus niveus degraded PBSA and PCL during 4-17 days. Lipase F-AP15 derived from Rhizopus orizae could degrade PBSA in 22 days. In these cases, PBS and PBSA were mainly degraded to dimers, whereas PCL was mainly degraded to monomers. Only poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (PHB/V) and poly (L-lactide) (PLA) were not degraded in the experiments. However, PLA degraded completely at 55 degrees C, pH 8.5 with Lipase PL during 20 days. This result could be explained with the sequential reactions of the chemical hydrolysis of the polymer to oligomers at higher pH and temperature, and the succeeding enzymatic hydrolysis of oligomers to the monomers.
ESTHER : Hoshino_2002_Biodegradation_13_141
PubMedSearch : Hoshino_2002_Biodegradation_13_141
PubMedID: 12449316