• Title/Summary/Keyword: Cadaverine

Search Result 68, Processing Time 0.031 seconds

Cadaverine is Transported into Vibrio vulnificus Through its CadB in Alkaline Environment

  • Kang, In-Hye;Kim, Eui-Jin;Lee, Jeong-K.
    • Journal of Microbiology and Biotechnology
    • /
    • v.19 no.10
    • /
    • pp.1122-1126
    • /
    • 2009
  • The exogenously added cadaverine is effective in protecting Vibrio vulnificus from methyl viologen (MV)-induced superoxide stress at pH 8.5. Such a protective effect by cadaverine was not observed at pH 7.5. Consistently, the accumulated level of intracellular cadaverine at pH 8.5 is approximately four times as much as that of the control cell at pH 7.5. Cadaverine accumulation is not affected by MV. The protection of V. vulnificus by cadaverine from superoxide stress was abolished when cadB coding for the lysine-cadaverine antiporter was interrupted. However, the cadaverine-mediated protection was complemented with cadB DNA. Therefore, CadB of V. vulnificus not only acts as a lysine-cadaverine antiporter at acid pH to neutralize the external medium, but also mediates cadaverine uptake at alkaline pH to result in cell protection from superoxide stress.

Analysis of Cadaverine and Its Worker Honeybee Venom Content (Apis mellifera L.) (꿀벌(Apis mellifera L.) 일벌독의 생체아민 cadaverine 함량 및 분석법)

  • Choi, Hong Min;Kim, Hyo Young;Kim, Se Gun;Han, Sang Mi
    • Journal of Life Science
    • /
    • v.31 no.2
    • /
    • pp.144-148
    • /
    • 2021
  • This study aimed to analyze the content and composition of a biological amine, cadaverine, isolated from the venom of worker honeybees (Apis mellifera L.). This biological amine―which has diverse functionality, such as anti-inflammatory and antibacterial effects―has not been previously reported in bee venom. An assay completed in 13 minutes was developed for the cadaverine present in the bee venom using an ultra-performance liquid chromatograph and a Halo C18 column with acetonitrile and water as the mobile phase. The specificity, accuracy, and precision of the assay were verified, and the assay was validated. The linearity for cadaverine in the bee venom was R2=0.99 or above, indicating a moderate level. The limit of detection and limit of quantification were both 0.3 ㎍/ml, and the rate of recovery was 97.6%-99.1%. The relative standard deviation (RSD) of the intra-day precision and inter-day precision for cadaverine was 0.25%-0.44% and 0.25%-1.25%, respectively, with an RSD that fell within 5% indicating excellent precision. Through this novel assay, it was found that the mean content of cadaverine was 1.10±0.05 mg/g. Our results indicated that the linearity, limit of detection, limit of quantification, and rate of recovery of the cadaverine assay were of a satisfactory level, and the cadaverine content of the bee venom was ably determined. This study provides basic data on cadaverine in bee venom, which will prove useful in further studies on the bioactivity of this component.

Cadaverine Protects Vibrio vulnificus from Superoxide Stress

  • Kang, In-Hye;Kim, Ju-Sim;Kim, Eui-Jin;Lee, Jeong
    • Journal of Microbiology and Biotechnology
    • /
    • v.17 no.1
    • /
    • pp.176-179
    • /
    • 2007
  • An electron paramagnetic resonance (EPR) signal characteristic of the 5,5'-dimethyl-l-pyrroline-N-oxide (DMPO)-OH spin adduct, which is formed from the reaction of DMPO with superoxide radicals generated by xanthine oxidasemediated reaction, was significantly reduced by the cadaverine or Escherichia coli Mn-containing superoxide dismutase (MnSOD). Likewise, cytochrome c reduction by superoxide was inhibited by cadaverine, and the inhibition level increased in proportion to the level of cadaverine. The cadA mutant of Vibrio vulnificus, which does not produce cadaverine because of the lack of lysine decarboxylase, exhibits less tolerance to superoxide stress in comparison with wild type. The results indicate that cadaverine scavenges superoxide radicals, and protects cells from oxidative stress.

$H_2O_2$-Bis(2,4,6-trichlorophenyl) Oxalate Chemiluminescence Detection of Monodansyl Cadaverine Derivatives of Free Fatty Acids in High Performance Liquid Chromatography (Monodansyl Cadaverine유도체화된 유리지방산류의 $H_2O_2$-Bis(2,4,6-trichlorophenyl) Oxalate에 의한 고속액체크로마토그라피)

  • 이용문;문동철
    • YAKHAK HOEJI
    • /
    • v.37 no.4
    • /
    • pp.362-364
    • /
    • 1993
  • The sensitive detection of free fatty acids was investigated by using H$_{2}$O$_{2}$-bis(2,4,6-trichlorophenyl) oxalate chemiluminescence system after monodansyl cadaverine labeling. Because dansvl moiety is well excited by this chemiluminescence system, monodansyl cadaverine was a prominent reagent to this system for the determination of free fatty acids. The cluent of 50mM tris-HCI buffer (pH 7.7)-acetonitrile (1:4, v/v) was run through TSK gel ODS 80 TM column. The reagent solutions were mixed with the eluent containing the monodansyl cadaverine derivative of fatty acids from the column. By this system, linolic acid was detected 50 fmol by injected amount.

  • PDF

Sensitive Fluorogenic Derivatization Method for Bile Acids by Dansyl Cadaverine (Dansyl Cadaverine을 이용한 담즙산류의 고감도 형광측정법)

  • Lee, Yong-Moon;Moon, Dong-Cheul;Han, Kun
    • Analytical Science and Technology
    • /
    • v.11 no.6
    • /
    • pp.429-435
    • /
    • 1998
  • Free and glycine conjugated bile acids were detected fluoromatrically in high-performance liquid chromatography after derivatization with dansyl cadaverine. The coupling agent, diethyl phosphorocyanidate was used to form the amide bond between dansyl cadaverine and analytes. The dansyl derivatives of 8 bile acids were separated successfully on Cosmosil ODS column by using linear gradient elution of 20% MeOH-water/$CH_3CN$. The detection limits of cholic acid was reached 10 pg(S/N=5) per $1{\mu}l$ of injected volume. This new derivatization method would be applicable to detect the changes of bile acids in biological samples.

  • PDF

Optimization of Direct Lysine Decarboxylase Biotransformation for Cadaverine Production with Whole-Cell Biocatalysts at High Lysine Concentration

  • Kim, Hyun Joong;Kim, Yong Hyun;Shin, Ji-Hyun;Bhatia, Shashi Kant;Sathiyanarayanan, Ganesan;Seo, Hyung-Min;Choi, Kwon Young;Yang, Yung-Hun;Park, Kyungmoon
    • Journal of Microbiology and Biotechnology
    • /
    • v.25 no.7
    • /
    • pp.1108-1113
    • /
    • 2015
  • Cadaverine (1,5-diaminopentane) is an important industrial chemical with a wide range of applications. Although there have been many efforts to produce cadaverine through fermentation, there are not many reports of the direct cadaverine production from lysine using biotransformation. Whole-cell reactions were examined using a recombinant Escherichia coli strain overexpressing the E. coli MG1655 cadA gene, and various parameters were investigated for the whole-cell bioconversion of lysine to cadaverine. A high concentration of lysine resulted in the synthesis of pyridoxal-5'-phosphate (PLP) and it was found to be a critical control factor for the biotransformation of lysine to cadaverine. When 0.025 mM PLP and 1.75 M lysine in 500 mM sodium acetate buffer (pH6) were used, consumption of 91% lysine and conversion of about 80% lysine to cadaverine were successfully achieved.

Cadaverine Production by Using Cross-Linked Enzyme Aggregate of Escherichia coli Lysine Decarboxylase

  • Park, Se Hyeon;Soetyono, Feilicia;Kim, Hyung Kwoun
    • Journal of Microbiology and Biotechnology
    • /
    • v.27 no.2
    • /
    • pp.289-296
    • /
    • 2017
  • Lysine decarboxylase (CadA) converts ${\small{L}}-lysine$ into cadaverine (1,5-pentanediamine), which is an important platform chemical with many industrial applications. Although there have been many efforts to produce cadaverine through the soluble CadA enzyme or Escherichia coli whole cells overexpressing the CadA enzyme, there have been few reports concerning the immobilization of the CadA enzyme. Here, we have prepared a cross-linked enzyme aggregate (CLEA) of E. coli CadA and performed bioconversion using $CadA^{CLEA}$. $CadA^{free}$ and $CadA^{CLEA}$ were characterized for their enzymatic properties. The optimum temperatures of $CadA^{free}$ and $CadA^{CLEA}$ were $60^{\circ}C$ and $55^{\circ}C$, respectively. The thermostability of $CadA^{CLEA}$ was significantly higher than that of $CadA^{free}$. The optimum pH of both enzymes was 6.0. $CadA^{free}$ could not be recovered after use, whereas $CadA^{CLEA}$ was rapidly recovered and the residual activity was 53% after the $10^{th}$ recycle. These results demonstrate that $CadA^{CLEA}$ can be used as a potential catalyst for efficient production of cadaverine.

Putrescine and Cadaverine Enhance Insulin Secretion of Mouse Pancreatic ${\beta}$-cell Line

  • Park, Hyo-Eun;Kim, Jae-Young
    • Biomedical Science Letters
    • /
    • v.18 no.3
    • /
    • pp.193-200
    • /
    • 2012
  • We examined the effects of polyamines such as putrescine and cadaverine on the biosynthesis and secretion of insulin in the mouse pancreatic ${\beta}$-cell line, MIN-6. Basal insulin secretion (BIS) and glucose-stimulated insulin secretion (GSIS) from the MIN-6 cells were significantly increased by 20 min- or 24 h-treatment with micromolar concentrations of polyamines. To determine whether the enhancement was due to increase of insulin production by polyamines, we investigated the insulin mRNA and protein production. Both insulin mRNA and protein production were found to be not significantly affected by the polyamine treatment. Next, we examined the expression of several transcription factors (TFs) related to insulin synthesis and secretion in order to identify upstream events responsible for the promotion of insulin secretion of MIN6 cells by polyamines. Of the 6 TFs tested, MafA was induced by treatment of polyamines. MafA mRNA and protein expressions increased with treatment of polyamines. Overall results suggest that cadaverine and putrescine promote the insulin secretion process rather than the insulin biosynthesis from MIN6 cells. Also MafA may be involved in the enhanced insulin secretion process. Further studies are needed to elucidate the underlying mechanisms for promotion of insulin secretion by polyamines.

Effects of Polyamine on the Self-splicing Inhibition of Group I Intron by Spectinomycin (Polyamine이 Spectinomycin에 의한 Group I Intron의 Splicing 억제에 미치는 영향)

  • Park, In-Kook
    • Korean Journal of Microbiology
    • /
    • v.35 no.4
    • /
    • pp.253-257
    • /
    • 1999
  • Effects of polyamines such as cadaverine, putrescine, spermidine and spermine on the self-splicig inhibition of the T4 phage thymidylate synthase(td) intron by spectinomycin have been investrigated. Without polyamine 7mM spectinomycin caused 40% reduction of the splicing rate. Cadaverine reduced the splicing rate over the concentrations of 0.1 to 5 mM. Putrescine at 0.5 mM increased the splicing rate by 13%. Spermidine at 0.5 mM enhanced the splicing rate by 11% while spermine at 0.01 mM enhanced the splicing rate by 16%. Of the all polyamines tested, spermine exhibited the maximum activation effect to counteract the splicing inhibition by spectinomycin. This effect appears to be due to the role of polyamine in stabilizing the conformation of td intron ribozyme essential for the catalytic function.

  • PDF

Functional Study of Lysine Decarboxylases from Klebsiella pneumoniae in Escherichia coli and Application of Whole Cell Bioconversion for Cadaverine Production

  • Kim, Jung-Ho;Kim, Hyun Joong;Kim, Yong Hyun;Jeon, Jong Min;Song, Hun Suk;Kim, Junyoung;No, So-Young;Shin, Ji-Hyun;Choi, Kwon-Young;Park, Kyung Moon;Yang, Yung-Hun
    • Journal of Microbiology and Biotechnology
    • /
    • v.26 no.9
    • /
    • pp.1586-1592
    • /
    • 2016
  • Klebsiella pneumoniae is a gram-negative, non-motile, rod-shaped, and encapsulated bacterium in the normal flora of the intestines, mouth, skin, and food, and has decarboxylation activity, which results in generation of diamines (cadaverine, agmatine, and putrescine). However, there is no specific information on the exact mechanism of decarboxylation in K. pnuemoniae. Specifically lysine decarboxylases that generate cadaverine with a wide range of applications has not been shown. Therefore, we performed a functional study of lysine decarboxylases. Enzymatic characteristics such as optimal pH, temperature, and substrates were examined by overexpressing and purifying CadA and LdcC. CadA and LdcC from K. pneumoniae had a preference for L-lysine, and an optimal reaction temperature of 37℃ and an optimal pH of 7. Although the activity of purified CadA from K. pneumoniae was lower than that of CadA from E. coli, the activity of K. pneumoniae CadA in whole cell bioconversion was comparable to that of E. coli CadA, resulting in 90% lysine conversion to cadaverine with pyridoxal 5'-phosphate L-lysine.