• New & Renewable Energy
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• v.18 no.3
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• pp.10-22
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• 2022

Forest biomass energy is based on scientific evidence in response to carbon neutrality and the climate crisis, international consensus, and environmental-geographic characteristics of each nation. In this study, the authors aimed to analyze macroscopic forest biomass energy policies for ten major countries. They categorized them into six detailed categories (Sustainable utilization, Cascading Uutilization, Replacement of fossil fuel/Carbon intensive products, Utilization of forest by-products/residues as the source of energy, Contribution to carbon-neutral/climate change, and Biomass combined with CCS/CCUS ). In addition, the surveyed nations have developed a policy consensus on the active use of forest biomass with sustainable forest management except for the cascading utilization category. Furthermore, the authors evaluated the mid to long-term plans of the Korean government for improvements in the policy and legal aspects. As a result, the authors derived four major directions that South Korea should approach strategically in the future (1) secure financial resources for sustainable forest management and stimulating investment in the timber industry, (2) promote unified policies to establish a bio-economy, (3) enhancement of the forest biomass energy system, and (4) reorganization and promotion of strategy centered on the opinions of field experts in internal and external instability.

• Journal of Animal Science and Technology
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• v.64 no.3
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• pp.397-408
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• 2022

Rinse & Chill^® technology (RCT) entails rinsing the vasculature using a chilled isotonic solution (3℃; 98.5% water and a blend of dextrose, maltose, and sodium phosphates) to rinse out the residual blood from the carcass. Infusion of pre-chilled solutions into intact animal carcasses immediately upon exsanguination is advantageous in terms of lowering the internal muscle temperature and accelerating chilling. This technology is primarily used for purposes of effective blood removal, favorable pH decline, and efficient carcass chilling, all of which improve meat quality and safety. Although RCT solution contains some substrates, the pre-rigor muscle is still physiologically active at the time of early postmortem and vascular rinsing. Consequently, these substrates are fully metabolized by the muscle, leaving no detectable residues in meat. The technology has been commercially approved and in continuous use since 2000 in the United States and since 1997 in Australia. As of January 2022, 23 plants have implemented RCT among the 5 countries (Australia, US, Canada, New Zealand, and Japan) that have evaluated and approved RCT. All plants are operating under sound Sanitation Standard Operation Procedures (SSOP) and a sound Hazard Analysis Critical Control Point (HACCP) program. No food safety issues have been reported associated with the use of this technology. RCT has been adapted by the meat industry to improve product safety and meat quality while improving economic performance. Therefore, this review summarizes highlights of how RCT technically works on a variety of animal types (beef, bison, pork, and lamb).

• Journal of Microbiology and Biotechnology
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• v.33 no.7
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• pp.949-954
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• 2023

Type III polyketide synthase (PKS) found in bacteria is known as 1,3,6,8-tetrahydroxynaphthalene synthase (THNS). Microbial type III PKSs synthesize various compounds that possess crucial biological functions and significant pharmaceutical activities. Based on our sequence analysis, we have identified a putative type III polyketide synthase from Nocardia sp. CS682 was named as ThnA. The role of ThnA, in Nocardia sp. CS682 during the biosynthesis of 1,3,6,8 tetrahydroxynaphthalene(THN), which is the key intermediate of 1-(α-L-(2-O-methyl)-6-deoxymannopyranosyloxy)-3,6,8-trimethoxynaphthalene (IBR-3) was characterized. ThnA utilized five molecules of malonyl-CoA as a starter substrate to generate the polyketide 1,3,6,8-tetrahydroxynaphthalene, which could spontaneously be oxidized to the red flaviolin compound 2,5,7-trihydroxy-1,4-naphthoquinone. The amino acid sequence alignment of ThnA revealed similarities with a previously identified type III PKS and identified Cys¹³⁸, Phe¹⁸⁸, His²⁷⁰, and Asn³⁰³ as four highly conserved active site amino acid residues, as found in other known polyketide synthases. In this study, we report the heterologous expression of the type III polyketide synthase thnA in S. lividans TK24 and the identification of THN production in a mutant strain. We also compared the transcription level of thnA in S. lividans TK24 and S. lividans pIBR25-thnA and found that thnA was only transcribed in the mutant.

• Analytical Science and Technology
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• v.21 no.6
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• pp.526-534
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• 2008

To determine the trace level of synthetic and natural hormones in food, the improvement of official analytical method and new development of simultaneous determination of hormones were established. On the basis of developed analytical method, the background level of natural hormones and distribution of residual hormones were monitored in meat. Target hormones were six natural hormones such as estrogens ($17{\beta}$-estradiol, $17{\alpha}$-estradiol, estrone), androgens ($17{\beta}$-testosterone, $17{\alpha}$-testosterone), and gestagens (progesterone) and three synthetic hormones such as DES, zeranol, and taleranol. These hormones were analyzed by gas chromatographymass spectrometry. Newly developed multi-residue analysis method was applied for meat sample which were collected from market in the capital region and monitored the presence of residues of synthetic and natural steroid hormones. No residue of synthetic hormones were detected and endogenous level of progesterone was detected in cattle, pig and liver samples tested.

• Bulletin of the Korean Chemical Society
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• v.26 no.5
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• pp.729-734
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• 2005

A sensitive and selective method for quantitation of sofalcone and its active metabolite in human plasma has been established using liquid chromatography-electrospray ionization tandem mass spectrometry (LC-ESI/MS/MS). Plasma samples were transferred into 96-well plate using an automated sample handling system and spiked with 10 $\mu$L of 2 $\mu$g/mL $d_3$-sofalcone and $d_3$-sofalcone metabolite solutions (internal standard), respectively. After adding 0.5 mL of acetonitrile to the 96-well plate, the plasma samples were then vortexed for 30 sec. After centrifugation, the supernatant was transferred into another 96-well plate and completely evaporated at 40 ${^{\circ}C}$ under a stream of nitrogen. Dry residues were reconstituted with mobile phase and were injected into a $C_{18}$ reversed-phase column. The limit of quantitation of sofalcone and its metabolite was 2 ng/mL, using a sample volume of 0.2 mL for analysis. The reproducibility of the method was evaluated by analyzing 10 replicates over the concentration range of 2 ng/mL to 1000 ng/mL. The validation experiments of the method have shown that the assay has good precision and accuracy. Sofalcone and its metabolite produced a protonated precursor ion ([M+H]$^+$) of m/z 451 and 453, and a corresponding product ion of m/z 315 and 317, respectively. Internal standard ($d_3$-sofalcone and $d_3$-sofalcone metabolite) produced a protonated precursor ion ([M+H]$^+$) of m/z 454 and 456 and a corresponding product ion of m/z 315 and 317, respectively. The method has been successfully applied to a pharmacokinetic study of sofalcone and its active metabolite in human plasma.

• Clean Technology
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• v.22 no.3
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• pp.175-180
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• 2016

Tyrosinases catalyze the hydroxylation of a monophenol (monophenolase activity) and the conversion of an o-diphenol to o-quinone (diphenolase activity), which are mainly involved in the modification of tyrosine residues into 3,4-dihydroxyphenyl-alanine (DOPA) and DOPA/DOPAquinone-derived intermolecular cross-linking. Previously, we obtained a slightly acidic and cold-active tyrosinase, tyrosinase-CNK, by our recombinant protein approach. The enzyme showed optimal activity at pH 6.0 and 20 ℃ with an abnormally high monophenolase/diphenolase activity ratio and still had approximately 50% activity compared with the highest activity even in ice water. Here, we investigated reaction stability of the recombinant tyrosinase-CNK as a psychrophilic enzyme. The enzyme showed remarkable thermal stability at 0 ℃ and the activity was well conserved in repeated freeze-thaw cycles. Although water-miscible organic solvent as reaction media caused the activity decrease of tyrosinase-CNK as expected, the enzyme activity was not additionally decreased with increased concentration in organic solvents such as ethanol and acetonitrile. Also, the enzyme showed high salt tolerance in chaotropic salts. It was remarkably considered that 2⁺ metal ions might inhibit the incorporation of Cu²⁺ into the active site. We expect that these results could be used to design tyrosinase-mediated enzymatic reaction at low temperature for the production of catechols through minimizing unwanted self-oxidation and enzyme inactivation.

• Journal of the Korean Society of Food Science and Nutrition
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• v.32 no.5
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• pp.752-757
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• 2003

This study was carried out in order to develop the method for isolation of red ginseng acidic polysaccharide (RGAP) haying immunomodulating antitumor activity from red ginseng by-product. The red ginseng by-product was obtained from red ginseng residues produced in processing of red ginseng ethanol extract. The yield of RGAP isolated by ultrafiltration was 20.9%. The active substance (GFP) was purified by DEAE-sepharose column chromatography RGAP induced nitric oxide (NO) exhibited tumoricidal activities against P8l5 (mastocytoma) tumor cells. Acid-hydrolyzed RGAP fragments were shown four to five spots. These sopts showed the same R$_{f}$ values with sugars designated as rhamnose, glucose, glactose and glucuronic acid. Some physico-chemical properties of RGAP were investigated. pH and dry reduction content at 105$^{\circ}C$ were 4.74 and 4.72%, respectively. Crude protein, ash and Pb contents were 3.30%, 4.74% and 2.30 ppm. These results suggest that we will be able to produce RGAP from red ginseng by-product by ultrafiltration in a large scale.e.

• Korean Journal of Microbiology
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• v.45 no.2
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• pp.200-207
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• 2009

In this study, the characterization of purified erythritol 4-phosphate dehydrogenase, key enzyme of erythritol biosynthesis, produced by Penicillium sp. KJ81 was investigated. Optimum production conditions of erythritol 4-phosphate dehydrogenase was 1 vvm areration, 200 rpm agitation, at $37^{\circ}C$ for 8 days in the medium containing 30% sucrose, 0.5% yeast extract, 0.5% $(NH_4)_2SO_4$, 0.1% $KH_2PO_4$, and 0.05%$MgCl_2$. Erythritol 4-phosphate dehydrogenase was purified through ultrafiltration and preparative gel electrophoresis from cell extract of Penicillium sp. KJ81. This enzyme was especially active on erythrose 4-phosphate with 1.07 mM of Km value. It gave a single band on native polyacrylamide gel electrophoresis and an isoelectric point of 4.6. The enzyme had an optimal activity at pH 7.0 and $30^{\circ}C$. It was stable between pH 4.0 and 9.0, and also below $30^{\circ}C$. The enzyme activity was completely inhibited by 1mM $Cu^{2+}$ and 1 mM $Zn^{2+}$, but was not significantly affected by other cations tested. This enzyme was inactivated by treatment of tyrosine specific reagent, iodine and tryptophan specific reagent, N-bromosuccinimide. The substrate of the enzyme, erythrose 4-phosphate showed protective effect on the inactivation of the enzyme by both reagents. These results suggest that tryptophan and tyrosine residues are probably located at or near active site of the enzyme.

• Applied Biological Chemistry
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• v.29 no.1
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• pp.90-95
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• 1986

A comparative study of chemical characteristics, efficacy and relative merits of extruded and coated granules, containing fungicide and insecticide, was conducted under laboratory and field conditions. Probenzole (3-allyloxy-1,2-benzisothiazole 1,1-dioxide) and carbofuran (2,3-dihydro-2,2-dimethyl-7-benzofuranyl methyl carbamate) were chosen as toxicants for rice blast(Pyricularia oryzae) and brown planthopper (Nilaparvata lugens) control, respectively. Stability of active ingredients in coated granule was superior to the extruded one under accelerated temperature. Active ingredient dissolution of coated one into distilled water showed slow release pattern. Pesticide residues in rice (Oryzae sativa, Chucheongbyeo) shoot applied with extruded one at the dosage of 3kg/10a retained higher levels than those with coated one on two days after application, while the residue levels were a reversed tendency on eight days after application. Efficacy on rice blast exhibited minute differences between the granules, on the other hand efficacy on brown planthopper by coated one was of higher rank than that by extruded one. Production cost of the combined pesticide granule by coating method could be cut down by 6% as compared to extrusion method.

• Journal of Life Science
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• v.27 no.9
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• pp.1003-1010
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• 2017

An open reading frame coding for mannanase predicted from the partial genomic sequence of Paenibacillus woosongensis was cloned into Escherichia coli by polymerase chain reaction amplification, and completely sequenced. This mannanase gene, designated man26AT, consisted of 3,162 nucleotides encoding a polypeptide of 1,053 amino acid residues. Based on the deduced amino acid sequence, Man26AT was identified as a modular enzyme, which included a catalytic domain belonging to the glycosyl hydrolase family 26 and two carbohydrate-binding modules, CBM27 and CBM11. The amino acid sequence of Man26AT was homologous to that of several putative mannanases, with identity of 81% for P. ihumii and identity of less than 57% for other strains of Paenibacillus. A cell-free extract of recombinant E. coli carrying the man26AT gene showed maximal mannanase activity at $55^{\circ}C$ and pH 5.5. The enzyme retained above 80% of maximal activity after preincubation for 1 h at $50^{\circ}C$. Man26AT was comparably active on locust bean gum (LBG), galactomanan, and kojac glucomannan, whereas it did not exhibit activity on carboxymethylcellulose, xylan, or para-nitrophenyl-${\beta}$-mannopyranoside. The common end products liberated from mannooligosaccharides, including mannotriose, mannotetraose, mannopentaose, and mannohexaose, or LBG by Man26AT were mannose, mannobiose, and mannotriose. Mannooligosacchrides larger than mannotriose were found in enzymatic hydrolyzates of LBG and guar gum, respectively. However, Man26AT was unable to hydrolyze mannobiose. Man26AT was intracellularly degraded into at least three active proteins with different molecular masses by zymogram.