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Optimal conditions for biological hydrogen production from food waste

  • Wongthanate, Jaruwan;Chinnacotpong, Kittibodee
    • Environmental Engineering Research
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    • v.20 no.2
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    • pp.121-125
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    • 2015
  • Biohydrogen production from food waste via dark fermentation was conducted by using mixed culture under various environmental conditions (initial pH, initial F/M ratio, initial ferrous iron ($Fe^{2+}$), and temperature condition) in batch reactor. The results revealed that the maximum hydrogen yield of $46.19mL\;H_2/g\;COD_{add}$ was achieved at the optimal conditions (initial pH 8.0, initial F/M ratio 4.0, initial iron concentration 100 mg $FeSO_4/L$ and thermophilic condition ($55{\pm}1^{\circ}C$)). Furthermore, major volatile fatty acid (VFA) productions of butyrate (765.66 mg/L) and acetate (324.69 mg/L) were detected and COD removal efficiency was detected at 66.00%. Therefore, these optimal conditions could be recommended to operate a system.

Phylogenetic relationships of Korean campanulaceae based on chloroplast DNA sequences (엽록체 DNA 염기서열 분석을 이용한 한국산 초롱꽃과 (Campanulaceae)의 계통유연관계)

  • Kim, Kyung-Ah;Yoo, Ki-Oug
    • Korean Journal of Plant Taxonomy
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    • v.42 no.4
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    • pp.282-293
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    • 2012
  • Phylogenetic studies were conducted to evaluate the taxonomic relationships among 28 taxa, including 2 outgroups of Korean Campanulaceae, using atpB, atpB-rbcL, atpF-H, matK, rbcL, rpl16, rpoC1 and trnL-F regions sequences in chloroplast DNA. The combined analyses of eight chloroplast DNA regions suggest that Codonopsis and Platycodon basally branches within the phylogenetic tree; Wahlenbergia distinguished an independent clade; Campanula forms a clade; Peracarpa and Asyneuma clade is a sister to the Adenophora-Hanabusaya clade; Hanabusaya is placed within the section Remotiflorae of Adenophora; Adenophora form a clade. Our present results support the generic level, although discordance remained at the infrageneric groups such as section and series based on morphological characteristics in the genus Adenophora.

Bioequivalence of Cefaclor (250 mg) Capsule (세파클러 250 mg 캅셀의 생물학적 동등성)

  • Yun, MH;Kim, HS;Choi, YP;Kwon, KI
    • Korean Journal of Clinical Pharmacy
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    • v.12 no.2
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    • pp.71-75
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    • 2002
  • This study was carried out to compare the bioavailability of $Ceclex^{(R)}$ (test drug, cefaclor 250 mg/capsule) with that of $Ceclor^{(R)}$ (reference drug) and to estimate the pharmacokinetic parameters of cefaclor in healthy Korean adult. The bioavailability was examined on 20 healthy volunteers who received a single dose (250 mg) of each drug in the fasting state in a randomized balanced 2-way crossover design. After dosing, blood samples were collected for a period of 6hours. Plasma concentrations of cefaclor were determined using HPLC with UV detection. The pharmacokinetic parameters $(AUC_{0-6hr},\;C_{max},\;T_{max},\;AUC_{int},\;K_e,\;t_{1/2},\;Vd)$ F, and CL/F) were calculated with non-compartmental pharmacokinetic analysis. The ANOVA test was utilized for the statistical analysis of the $T_{max},\;log-transformed\;AUC_{0-6hr}\;log-transformed\;C_{max},\;t_{l/2},\;V_d/F$, and CL/F. The ratios of geometric means of AUC0-6hr and $C_{max}$ between test drug and reference drug were $103.2\%\;(6.74\;{\mu}g{\cdot}hr/ml\;vs\;6.53{\pm}g{\cdot}hr/ml)\;and\;100.4\%\;(4.85\;{\mu}g\ml\;vs\;4.82\;{\mu}g/ml)$, respectively. The $T_{max}$ of test drug and reference drug were $0.9\pm0.38\;hr\;and\;0.83\pm0.34$ hrs, respectively. The $90\%$ confidence intervals of mean difference of logarithmic transformed $AUC_{0-6h},\;and\;C_{max}$ were log $0.98{\sim}log$ 1.08 and log $0.88{\sim}log1.15$, respectively. It shows that the bioavailability of test drug is equivalent with that of reference drug. The estimated half-life of this study was longer $(1.21\pm0.27\;hrs\;vs\;0.5-1\;hr)$, the Vd/F was larger $(68.89\pm25.72L$ vs 24.9L), and the CL/F was higher $(38.62\pm7.09\;L/hr$ vs 24.9 L/hr) than the previously reported values.

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Mass Culture and Dietary Value of Fabrea salina (Fabrea salina의 대량배양과 먹이효율)

  • PARK Chul Hyun;HUR Sung Bum
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.34 no.1
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    • pp.32-37
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    • 2001
  • Fabrea salina is an euryhaline ciliate living at salt pond. Its size is small as ca. $150{\mu}m$, and its reproductive rate is high, so that this ciliate has been expected to be a new food organism which will be able to replace rotifer, Brachionus plicatilis. However, the dietary value of F. salina on fish larvae has not yet been verified thoroughly. This research was carried out to understand the mass culture technique and dietary value of this ciliate. In this study, six kinds of phytoplankton and three kinds of grain were tested on growth of the ciliate and optimum temperature, salinity and density of food were also examined for its mass culture. Regarding food for the ciliate, Heterosigma sp. and rice showed the highest growth among the phytoplankton and the grain, respectively. In this study, 229 ciliates per mL was cultured with Heterosigma sp., and 220 ciliates per mL with rice. The optimum temperature for F. salina was $33^{\circ}C$, and salinity ranging from 35 to 95 ppt had no significant difference on its growth. The optimum food density and amount for the ciliate were $5\times10^6$ cells/mL in Heterosigma sp. and 2.8 g/L in rice, respectively. With respect to dietary value of F. salina, six-day-old larvae of ayu, Plecoglossus altivelis, fed on the ciliate showed the high mortality over $96\%$ within 3 days, and it was significantly higher than those fed on rotifer. Even though the mass culture of F. salina has been achieved in the study, this ciliate seems to be inadequate as a food organism for fish larvae.

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Synthesis and Structure of [Cu(L)](ClO4)2 (L;3,5,10,12-Tetramethyl-1,4,8,11-tetraazacyclotetradecane) ([Cu(L)](ClO4)2 (L:3,5,10-12-Tetramethyl-1,4,8,11-tetraazacyclotetradecane) 착물의 합성 및 구조)

  • 최기영;홍청표
    • Korean Journal of Crystallography
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    • v.9 no.1
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    • pp.6-10
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    • 1998
  • The complex[Cu(L)](ClO4)2 (1) (L:3,5,10,12-Tetramethyl-1,4,8,11-tetraazacyclotetradecane) has been synthesized and structurally characterized. The complex 1 crystallizes in the monoclinic system, space group P21/n with cell parameters a=8.208(2)Å, b=13.339(6) Å, c=10.752(5) Å, β=111.02(4)˚ Z=2. Least-squares refinement of 1 led to a R(RW)factor of 0.073 (0.142) for 617 observed reflections of F0>40(F0). The crystal structure of 1 has a square-planar geometry and adopts the trans-III conformation.

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Functional Characterization of Pharmcogenetic Variants of Human Cytochrome P450 2C9 in Korean Populations

  • Cho, Myung-A;Yoon, Jihoon G.;Kim, Vitchan;Kim, Harim;Lee, Rowoon;Lee, Min Goo;Kim, Donghak
    • Biomolecules & Therapeutics
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    • v.27 no.6
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    • pp.577-583
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    • 2019
  • Human cytochrome P450 2C9 is a highly polymorphic enzyme that is required for drug and xenobiotic metabolism. Here, we studied eleven P450 2C9 genetic variants-including three novel variants F69S, L310V, and Q324X-that were clinically identified in Korean patients. P450 2C9 variant enzymes were expressed in Escherichia coli and their bicistronic membrane fractions were prepared The CO-binding spectra were obtained for nine enzyme variants, indicating P450 holoenzymes, but not for the M02 (L90P) variant. The M11 (Q324X) variant could not be expressed due to an early nonsense mutation. LC-MS/MS analysis was performed to measure the catalytic activities of the P450 2C9 variants, using diclofenac as a substrate. Steady-state kinetic analysis revealed that the catalytic efficiency of all nine P450 2C9 variants was lower than that of the wild type P450 2C9 enzyme. The M05 (R150L) and M06 (P279T) variants showed high $k_{cat}$ values; however, their $K_m$ values were also high. As the M01 (F69S), M03 (R124Q), M04 (R125H), M08 (I359L), M09 (I359T), and M10 (A477T) variants exhibited higher $K_m$ and lower $k_{cat}$ values than that of the wild type enzyme, their catalytic efficiency decreased by approximately 50-fold compared to the wild type enzyme. Furthermore, the novel variant M07 (L310V) showed lower $k_{cat}$ and $K_m$ values than the wild type enzyme, which resulted in its decreased (80%) catalytic efficiency. The X-ray crystal structure of P450 2C9 revealed the presence of mutations in the residues surrounding the substrate-binding cavity. Functional characterization of these genetic variants can help understand the pharmacogenetic outcomes.

Suppression of a Residue 173 Mutant Form on Aggregation of Tryptophan Synthase α-Subunits from Escherichia coli (대장균 트립토판 중합효소 α 소단위체의 응집 형성에 미치는 잔기 173 치환체의 억제 효과)

  • Jeong, Jae Kap;Park, Hoo Hwi;Lim, Woon Ki
    • Journal of Life Science
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    • v.32 no.9
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    • pp.729-733
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    • 2022
  • Aggregation of normally soluble proteins can cause disease-related problems. Tryptophan synthase α-subunit (αTS) in E. coli adopts one of most popular structural scaffolds, the TIM barrel fold. Previous mutagenesis of the αTS gene resulted in many aggregation-prone mutant proteins. Here, Y173F (Tyr at residue 173 to Phe) substitution, which imparts increased stability, was tested for its ability to suppress aggregation of aggregation-prone mutant proteins (Y4C, S33L, P28L, P28S, G44S, D46N, P96L, and P96S). Aggregation was suppressed in all eight severe aggregate-forming mutants (all differing in their mutation positions), by the Y173F replacement. P28L αTS, which was available in pure form, was further analyzed and showed reduced secondary structure content, lower stability, and a looser structure with more exposed hydrophobic surface compared to the wild type protein. A double mutant P28L/Y173F protein showed almost no indication of these changes compared to the wild type protein. We hypothesized that Tyr at position 173 in αTS is positioned at the hydrophobic core and may serve to suppress the aggregation of this protein caused by other residues. Important residue (s) could be working widely in the prevention/suppression of protein aggregation.

X-ray Absorption and Photoemission Spectroscopy Study of Nd1/2A1/2Mn1-yCryO3(A=Ca, Sr)

  • Kang, J.S.;Kim, J.H.;Han, S.W.;Kim, K.H.;Choi, E.J.;Sekiyama, A.;Kasai, S.;Suga, S.;Kimura, T.
    • Journal of Magnetics
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    • v.8 no.4
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    • pp.142-145
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    • 2003
  • Valence states and electronic structures of Cr-doped $Nd_{1/2}A_{1/2}Mn_{1-y}Cr_{y}O_3$(NAMO; A=Ca, Sr) manganites have been investigated using x-ray absorption spectroscopy (XAS) and high-resolution photoemission spectroscopy (PES). All the Cr-doped NAMO systems exhibit the clear metallic Fermi edges in the Mn $e_{g}$ PES spectra near $E_{F}$. The spectral intensity at $E_{F}$ is higher for Cr-doped N $d_{l}$ 2/S $r_{l}$ 2/Mn $O_3$(NSMO) than for Cr-doped N $d_{l}$ 2/C $a_{l}$ 2/Mn $O_3$ (NCMO), reflecting the stronger metallic nature for NSMO than for NCMO. The measured Cr 2p XAS spectra are found to be very similar to that of C $r_2$ $O_3$, indicating that Cr ions in Cr-doped NAMO are in the trivalent C states ( $t^3$$_{2g}$). The Cr 2p XAS data are consistent with the Cr 3d PES spectra located at ∼1.3 eV below $E_{F}$ and having no emission near $E_{F}$.

Purification and Characterization of a Protease Produced by a Planomicrobium sp. L-2 from Gut of Octopus vulgaris

  • Liu, Qing;Sun, Shujing;Piao, Meizi;Yang, Ji Young
    • Preventive Nutrition and Food Science
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    • v.18 no.4
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    • pp.273-279
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    • 2013
  • Protease widely exists in the digestive tract of animals and humans, playing a very important role in protein digestion and absorption. In this study, a high protease-producing strain Planomicrobium sp. L-2 was isolated and identified from the digestive tract of Octopus variabilis. The strain was identified by physiological and biochemical experiments and 16S rDNA sequences analysis. A protease was obtained from the strain Planomicrobium sp. L-2 through ammonium sulfate precipitation, dialysis and enrichment, DEAE-Sephadex A50 anion-exchange chromatography, and Sephadex G-100 gel chromatography. The molecular weight and properties of the protease were characterized, including optimum temperature and pH, thermal stability, protease inhibitions and metal ions. According to our results, the protease from Planomicrobium sp. L-2 strain designated as F1-1 was obtained by three-step separation and purification from crude enzyme. The molecular weight of the protease was 61.4 kDa and its optimum temperature was $40^{\circ}C$. The protease F1-1 showed a broad pH profile for casein hydrolysis between 5.0~11.0. No residual activity was observed after incubation for 40 min at $60^{\circ}C$ and 60 min at $50^{\circ}C$. F1-1 protease was inhibited by $Mn^{2+}$, $Hg^{2+}$, $Pb^{2+}$, $Zn^{2+}$, and $Cu^{2+}$ ions, as well as PMSF, indicating that the protease F1-1 was a serine protease. Additionally, research basis provided by this study could be considered for industrial application of octopus intestinal proteases.

Metabolite Chemical Composition of the Bletilla striata (Thunb.) Reichb. f. Endophyte Penicillium oxalicum

  • Ran Liu;Xuehua Han;Jing Gao;Min Luo;Dale Guo;Guangzhi Wang
    • Mycobiology
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    • v.51 no.3
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    • pp.148-156
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    • 2023
  • Penicillium oxalicum strain can be isolated from the Bletilla striata (Thunb.) Reichb. f. tubers. Its solid-state fermentation products are concentrated by percolation extraction. Separation and purification have been conducted to the ethyl acetate extracts by preparative HPLC. Based on the use of spectrometry, we have determined 17 known compounds, 12,13-dihydroxy-fumitremorgin C (1), pseurotin A (2), tyrosol (3), cyclo-(L-Pro-L-Val) (4), cis-4-hydroxy-8-O-methylmellein (5), uracil (6), cyclo-(L-Pro-L-Ala) (7), 1,2,3,4-tetrahydro-4-hydroxy-4-quinolin carboxylic acid (8), cyclo-(Gly-L-Pro) (9), 2'-deoxyuridine (10), 1-(b-D-ribofuranosyl)thymine (11), cyclo-(L-Val-Gly) (12), 2'-deoxythymidine (13), cyclo-(Gly-D-Phe) (14), cyclo-L-(4-hydroxyprolinyl)-D-leucine (15), cyclo-(L)-4-hydroxy-Pro-(L)-Phe (16), uridine (17). Here, we report compounds 1-3, 5, 7-8, 11-12, 14-17 are first found and isolated from this endophyte.