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T Nakajima-Kambe

Publications and source records attributed to T Nakajima-Kambe.

12 recordsLinked to original sources
PubMed2004

Inhibition of matrix metalloproteinase-2 activity by siderophores of Pseudomonas species.

To obtain a novel matrix metalloproteinase (MMP) inhibitor produced by bacteria, we have focused on the chelating activity of siderophores. Several siderophore-producing bacteria were isolated from soil using chrome azurol S agar plates and then the effect of siderophores on MMP-2 activity was assayed by gelatin zymography. The results showed that partially purified siderophores from ten isolated strains inhibited MMP-2 activity. Among these strains, two were non-fluorescent and eight were fluorescent Pseudomonas species. From these eight strains, pyoverdine-type siderophores were detected. The Zn(2+)-chelating activity of these siderophores correlated with the inhibition of MMP-2 activity. Therefore, it is considered that siderophores such as pyoverdines inhibit MMP-2 activity by chelating Zn(2+) on the active site of MMP-2.

Binding Sites↗
PubMed2003

Isolation and characterization of a bacterium that degrades various polyester-based biodegradable plastics.

Microorganisms isolated from soil samples were screened for their ability to degrade various biodegradable polyester-based plastics. The most active strain, designated as strain TB-13, was selected as the best strain for degrading these plastics. From its phenotypic and genetic characteristics, strain TB-13 was closely related to Paenibacillus amyloyticus. It could degrade poly(lactic acid), poly(butylene succinate), poly(butylene succinate-co-adipate), poly(caprolactone) and poly(ethylene succinate) but not poly(hydroxybutylate-co-valerate). However, it could not utilize these plastics as sole carbon sources. Both protease and esterase activities, which may be involved in the degradation of plastic, were constitutively detected in the culture broth.

Adipates↗
PubMed2000

Properties of a bacterium which degrades solid poly(tetramethylene succinate)-co-adipate, a biodegradable plastic.

Various microorganisms were screened for their ability to degrade poly(tetramethylene succinate)-co-(tetramethylene adipate) (PBSA). Strain BS-3, which was newly isolated from a soil sample, was selected as the best strain. From taxonomical studies, the strain was tentatively ascribed to belong to the genus Acidovorax, most probably to the species A. delafieldii. Strain BS-3 could degrade both solid and emulsified PBSA, and also emulsified poly(tetramethylene succinate). During the degradation, a lipase activity was observed in the culture broth. This lipase activity was induced more strongly by PBSA than by tributyrin or triolein which are typical substrates of lipase. These observations strongly suggest that this lipase was involved in the PBSA biodegradation in strain BS-3.

Adipates↗
PubMed2000

Cloning and expression of genes encoding meta-cleavage enzymes from 4,6-dimethyldibenzothiophene-degrading Sphingomonas strain TZS-7.

Sphingomonas strain TZS-7 was reported as the first strain to have the ability to degrade 4,6-dimethyldibenzothiophene (4,6-dmDBT) by the ring-destructive pathway. Two genes for meta-cleavage dioxygenases were cloned from strain TZS-7. Expression of each gene showed that one enzyme was specific for 2,3-dihydroxybiphenyl while another was more specific for catechol. The genes for the two enzymes were named dmdC and catA. The analysis of deduced amino acid sequences indicates that CatA falls into the class of meta-cleavage dioxygenases acting on dihydroxylated monocyclic compounds and DmdC falls into the class of meta-cleavage dioxygenases acting on dihydroxylated polycyclic compounds.

Amino Acid Sequence↗
PubMed2000

Efficient conversion of itaconic acid to (S)-(+)-citramalic acid by Alcaligenes xylosoxydans IL142.

The effective production of (S)-(+)-citramalic acid from itaconic acid with an enantiomeric purity of more than 99.9% was successfully achieved using resting cells of a newly isolated strain, Alcaligenes xylosoxydans IL142. The highest conversion activity was obtained with an itaconic acid concentration of 65.0 g.l(-1). After 30 h of reaction, 68.9 g.l(-1) of (S)-(+)-citramalic acid was produced from 65.0 g.l(-1) of itaconic acid. This is equivalent to a molar yield of 93.1%. This production process is of considerable economic significance because only very few by-products were detected. The ATP and CoA requirements for (S)-(+)-citramalic acid formation from itaconic acid were evaluated using crude cell-free enzymes. Addition of succinate enhanced the production of (S)-(+)-citramalic acid in the presence of CoA and ATP. These results suggest the existence of strong citramalyl-CoA transferase activity in the cell.

Journal Article↗
PubMed1999

Microbial degradation of polyurethane, polyester polyurethanes and polyether polyurethanes.

Polyurethane (PUR) is a polymer derived from the condensation of polyisocyanate and polyol and it is widely used as a base material in various industries. PUR, in particular, polyester PUR, is known to be vulnerable to microbial attack. Recently, environmental pollution by plastic wastes has become a serious issue and polyester PUR had attracted attention because of its biodegradability. There are many reports on the degradation of polyester PUR by microorganisms, especially by fungi. Microbial degradation of polyester PUR is thought to be mainly due to the hydrolysis of ester bonds by esterases. Recently, polyester-PUR-degrading enzymes have been purified and their characteristics reported. Among them, a solid-polyester-PUR-degrading enzyme (PUR esterase) derived from Comamonas acidovorans TB-35 had unique characteristics. This enzyme has a hydrophobic PUR-surface-binding domain and a catalytic domain, and the surface-binding domain was considered as being essential for PUR degradation. This hydrophobic surface-binding domain is also observed in other solid-polyester-degrading enzymes such as poly(hydroxyalkanoate) (PHA) depolymerases. There was no significant homology between the amino acid sequence of PUR esterase and that of PHA depolymerases, except in the hydrophobic surface-binding region. Thus, PUR esterase and PHA depolymerase are probably different in terms of their evolutionary origin and it is possible that PUR esterases come to be classified as a new solid-polyester-degrading enzyme family.

Bacteria↗
PubMed1999

Biodegradation of dibenzothiophene and 4,6-dimethyldibenzothiophene by Sphingomonas paucimobilis strain TZS-7.

Strain TZS-7, tentatively identified as Sphingomonas paucimobilis, was isolated from crude oil for its ability to degrade dibenzothiophene (DBT) and 4,6-dimethyldibenzothiophene (4,6-dmDBT). This strain did not utilize DBT or 4,6-dmDBT as the sole source of sulfur. However, the degradative activity was induced by various aromatic compounds, including DBT, fluorene, anthracene, naphthalene and toluene. Three products formed from 4,6-dmDBT degradation were detected and two of these were proposed to be 7-methyl-3-hydroxy-2-formylbenzothiophene and 7-methylbenzothiophene-2,3-dione by gas chromatography-mass spectrometry analysis. These findings proved that 4,6-dmDBT is degraded through a ring-destructive pathway by resting cells of strain TZS-7.

Journal Article↗
PubMed1999

Purification and properties of culture-broth-secreted esterase from the polyurethane degrader Comamonas acidovorans TB-35.

The polyester-polyurethane (PUR)-degrading bacterium Comamonas acidovorans TB-35 produces two kinds of esterases, one cell-bound esterase (PUR esterase) and the other secreted in the culture broth (CBS esterase). In this study, the CBS esterase and the two recombinant esterases were purified. Identification of the physical and biochemical properties of the CBS and PUR esterases revealed that they have the same polypeptide from one gene. This finding was supported by the observation that Escherichia coli harboring the PUR esterase gene also produced two kinds of esterases. Though the PUR esterase degraded PUR and poly(diethylene glycol adipate), the soft segment of the PUR, the CBS esterase degraded only poly(diethylene glycol adipate). Furthermore, the hydrophobicity of the CBS esterase was lower than that of the PUR esterase. As the PUR esterase has been previously indicated to possess a PUR-binding domain, it was assumed that structural change around the PUR-binding domain of the CBS esterase was responsible for its inability to degrade PUR.

Journal Article↗
PubMed1999

Decolorization of molasses wastewater by Bacillus sp. under thermophilic and anaerobic conditions.

Various microorganisms were screened for their ability to decolorize molasses wastewater under thermophilic and anaerobic conditions. Strain MD-32, which was newly isolated from a soil sample, was selected as the best strain. From taxonomical studies, the strain was concluded to belong to the genus Bacillus, most closely resembling B. smithii. The strain decolorized 35.5% of molasses pigment within 20 d at 55 degrees C under anaerobic conditions, but no decolorization activity was observed when it was cultivated aerobically. At all the concentrations tested molasses pigment was effectively decolorized by MD-32, with decolorization yields of around 15% within 2 d. The molecular weight distribution as determined by gel filtration chromatography revealed that the decolorization of molasses pigment by the isolated strain is accompanied by a decrease in not only small molecules but also large ones.

Journal Article↗
PubMed1998

Purification and Properties of a Polyester Polyurethane-Degrading Enzyme from Comamonas acidovorans TB-35.

A polyester polyurethane (PUR)-degrading enzyme, PUR esterase, derived from Comamonas acidovorans TB-35, a bacterium that utilizes polyester PUR as the sole carbon source, was purified until it showed a single band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). This enzyme was bound to the cell surface and was extracted by addition of 0.2% N,N-bis(3-d-gluconamidopropyl)deoxycholamide (deoxy-BIGCHAP). The results of gel filtration and SDS-PAGE showed that the PUR esterase was a monomer with a molecular mass of about 62,000 Da. This enzyme, which is a kind of esterase, degraded solid polyester PUR, with diethylene glycol and adipic acid released as the degradation products. The optimum pH for this enzyme was 6.5, and the optimum temperature was 45 degrees C. PUR degradation by the PUR esterase was strongly inhibited by the addition of 0.04% deoxy-BIGCHAP. On the other hand, deoxy-BIGCHAP did not inhibit the activity when p-nitrophenyl acetate, a water-soluble compound, was used as a substrate. These observations indicated that this enzyme degrades PUR in a two-step reaction: hydrophobic adsorption to the PUR surface and hydrolysis of the ester bond of PUR.

Journal Article↗
PubMed1995

Isolation and characterization of a bacterium which utilizes polyester polyurethane as a sole carbon and nitrogen source.

Various soil samples were screened for the presence of microorganisms which have the ability to degrade polyurethane compounds. Two strains with good polyurethane degrading activity were isolated. The more active strain was tentatively identified as Comamonas acidovorans. This strain could utilize polyester-type polyurethanes but not the polyether-type polyurethanes as sole carbon and nitrogen sources. Adipic acid and diethylene glycol were probably the main degradation products when polyurethane was supplied as a sole carbon and nitrogen source. When ammonium nitrate was used as nitrogen source, only diethylene glycol was detected after growth on polyurethane.

Biodegradation, Environmental↗