• Journal of Microbiology and Biotechnology
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• v.12 no.5
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• pp.729-734
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• 2002

Radiorespirometric analysis revealed that Pseudomonas sp. strain KKI isolated from a soil contaminated with petroleum hydrocarbons was able to catabolize polycyclic aromatic hydrocarbons such as phenanthrene and naphthalene. The rate and extent of phenanthrene mineralization was markedly enhanced when the cells were pregrown on either naphthalene or phenanthrene, compared to the cells grown on universal carbon sources (i.e., TSA medium). Deduced amino acid sequence of the Rieske-type iron-sulfur center of a putative phenanthrene dioxygenase (PhnAl) obtained from the strain KKI shared significant homology with DxnAl (dioxin dioxygenase) from Spingomonas sp. RW1, BphA1b (biphenyl dioxygenase) from Spingomonas aromaticivorans F199, and PhnAc (phenanthrene diokygenase) from Burkholderia sp. RP007 or Alcaligenes faecalis AFK2. Northern hybridization using the dioxygenase gene fragment cloned from KKI showed that the expression of the putative phn dioxygenase gene reached the highest level in cells grown in the minimal medium containing phenanthrene and $KNO_3$, and the expression of the phn gene was repressed in cells grown with glucose. In addition to the metabolic change, phospholipid ester-linked fatty acids (PLFA) analysis revealed that the total cellular fatty acid composition of KKI was significantly changed in response to phenanthrene. Fatty acids such as 14:0, 16:0 3OH, 17:0 cyclo, 18:1$\omega$7c, 19:0 cyclo increased in phenanthrene-exposed cells, while fatty acids such as 10:0 3OH, 12:0, 12:0 2OH, 12:0 3OH, 16:1$\omega$7c, 15:0 iso 2OH, 16:0, 18:1$\omega$6c, 18:0 decreased.

• Journal of the Korean Chemical Society
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• v.38 no.8
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• pp.608-615
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• 1994

The isolation, purification and characterization of a carotenoprotein from the carapace of Pnaeus orientalis were investigated. The carotenoprotein was purple with broad λmax between 480, 409, 318 and 280 nm. Apparent structures were estimated by using X-ray diffractometry and scanning electron microscope, respectively. The molecular weight of the carotenoprotein complex had been determined by GPC and PAGE. The heavier complex, designated the $\alpha$-form (M.W = 170 KDa), was dissociated to a major subunit, $\beta$-form (M.W = 42 KDa). SDS-PAGE of $\alpha$-form showed apparently oligomeric pattern, and also $\beta$-form gave two polypeptides corresponding to 22 KDa and 19 KDa, respectively. The amino acid of the two proteins $({\alpha}-and\;{\beta})$-form, lipid and free fatty acid compositions were described. The prosthetic groups of the carotenoprotein were confirmed by TLC, IR, $^1H$-NMR, MS and various organic reactions as astaxanthin, astaxanthin monoester and astaxnathin diester.

• Korean Journal of Food Science and Technology
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• v.15 no.2
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• pp.128-132
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• 1983

The apple seed contained 25.96% of crude fat and 37.62% of crude protein. The lipid fractions obtained by cilicic column chromatography were mainly composed of about 93.52% neutral lipid, whereas compound lipid was only 6.48% level. Among the neutral lipid separated by thin layer chromatography, triglyceride was 92.17%, sterol ester, sterol, diglyceride and free fatty acid were 3.53, 2.25, 1.44 and 0.56, respectively. The predominent fatty acids of total and neutral lipids were linoleic acid (59.79-69.37%) and oleic acid (20.04-29.82%), but those of glycolipid and phojspholipid were linoleic acid (29.20-36.04%). The major fatty acids of triglyceride separated from neutral lipid were oleic acid (44.31%), linoleic acid (36.66%) and palmitic acid (12.48%). The salt soluble protein of apple seed was highly dispersible in 0.02M sodium phosphate buffer containing about 1.0M $MgSO_4$, and the extractability of seed protein was 37%, Glutamic acid was the major amino acid in salt soluble protein, followed by arginine and aspartic acid. The eletrophoretic analysis showed three bands in apple seed protein, and the collection rate of the main protein fraction purified by Sephadex G-100 and G-200 was 76.6%. Glutamic acid, aspartic acid and arginine were the major amino acids of the main apple seed protein. The molecular weight for the main protein of the apple seed was estimated to be 45,000.

• Journal of the Korean Society of Food Science and Nutrition
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• v.12 no.1
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• pp.46-50
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• 1983

In order to find out the possibility of utilizing red pepper seed as food resources of fats and proteins, a series of studies were conducted. The red pepper seed contained 27.6% of crude fat and 22.2% of crude protein. The lipid fractions obtained by silicic acid column chromatography were mainly composed of 95.4% neutral lipid, where as compound lipid were 4.6%. Among the neutral lipid separated by thin layer chromatography, triglyceride was 85.6%, sterol ester 4.9%, free fatty acids 3.4%, diglyceride 2.5%, sterol 2.2% and monoglyceride 1.1%, respectively. The predominant fatty acids of red pepper seed oil were linoleic acid (57.1-75.4%), palmitic acid (13.9-21.3%) and oleic acid (8.0-15.1%), especially glycolipid contained 1.7% of linolenic acid and small amount of myristic acid and arachidic acid. The salt soluble protein of red pepper seed was highly dispersible in 0.02M sodium phosphate buffer containing 1.0M $MgSO_4$, and the extractability of seed protein was about 25.0%. Glutamic acid and arginine were major amino acids of red pepper seed protein. The electrophoretic analysis showed 6 bands in seed protein, and the collection rate of the main protein fraction purified by sephadex G-100 and G-200 was about 62.2%. Glutamic acid (19.9%) was major amino acid of the main protein, followed by glycine and alanine. The molecular weight of the main protein was estimated to be 93,000.

• Microbiology and Biotechnology Letters
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• v.38 no.1
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• pp.46-52
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• 2010

Yakju, a Korean traditional alcoholic beverage, is made from glutinous-rice flour or rice starch with nuruk. In this study, we investigated that fermentation characteristics in yakju was made with glutinous rice and pretreatment. The yeast and nuruk were used Y90-9 and SP1800 (a kind of improved nuruk), respectively. pH and brix degree of yakju, brewed with glutinous rice flour by heating, were higher than the others during fermentation process. Total acid contents were 0.2~0.3 and the highest alcohol degree (15.75%(v/v)) was fermented glutinous rice flour by heating. Reducing sugar contents were 3.5-3.9 mg/mL. Yakju, which brewed with glutinous rice flour, of amino acid degree, UV absorbance and color degree was higher than yakju which brewed with glutinous rice starch. Succinic acid was the highest organic acid among 6 organic acids and free sugar contents described as glucose > maltose > fructose. Twenty one components were identified including 3 alcohols, 17 esters and one aldehyde. Of these, ethyl palmitate, which was described as mild flavor, was the highest %area except ethyl alcohol. Overall, the fermentation performed using glutinous rice flour by heating and improved-nuruk showed the best results for yakju production.

• Korean Journal of Microbiology
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• v.35 no.2
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• pp.133-138
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• 1999

Essential amino acids involving in the active site ofthe cytidn~e deruninase from Bncillus subtilis ED 213 were determined by chemical modification studies. Tllc purified cytidine deruninase tiom Booillus subtilis ED 213 required the reduced form of Fe(lI)ion. since the enzyme was inhibited 43% by 1 mnM o-phenanthroline. Whereas the enzyme activity was activated up to 28% by 1 1 ethylenediaminetetraacetic acid. The cytidine deaninase activily was completely inhibited by 1 mM N-bromosuccinimide, chloramine-T, and p-chloromercuribenzoic acid (p-CMB), respectively. The enzyme activity was inhibited 36% by 1 mM pyridoxal-S-phosphale, and 31% by 1 mM l-ethy~-3-(3-dirneIhj~laminoprop}~~)c~bodiiamide and glycine inethyl ester. The enzyme activity was strongly inhibited 68% by 1 \mu$M \rho$-CMB and this inhibition of the enzyme activity with 1 \mu$M \rho$-CMB was completely reactivated by 5 mM cysleine as a reducing agent. We speculaled that tyrosine, methionine, cysteuie and/or serine residues are located ui or near ihe active site of the cytidine deruniuase from Bncilus subrilis ED 213 and indirectly related to lysine and/or glycine.

• Macromolecular Research
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• v.12 no.6
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• pp.581-585
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• 2004

A copolymer P[OSA-MI] was synthesized by copolymerization of its corresponding monomers, N-phenyl maleimide (MI) and 2-octen-l-ylsuccinic anhydride (OSA). The polymer (poly[2-[1-(2,5-dioxo-l-phenylpyrroli­din-3-ylmethyl)heptyl]-succinic acid 4-(2-$\{$ethyl-[4-(4-nitrophen-ylazo)phenyl]amino$\}$ethyl)ester]) P[DR1MA-MI] was obtained from the reaction of P[OSA-MI] with 2-[4-(4-nitrophenylazo)-N-ethylphenylamino] ethanol (DR1). A stable monolayer of P[DRIMA-MI] was formed by spreading the solution of the polymer in chloroform. In Y-type Langmuir-Blodgett (LB) films prepared using this Langmuir-Blodgett method, the second harmonic waves generated from adjacent mono layers canceled each other out. In X-and Z-type LB films, the second harmonic intensity increased upon increasing the number of monolayers, but this increase was somewhat smaller than predicted by the square law. This phenomenon is due to defects or imperfect alignment of the dipoles in the LB film. The generation of second harmonic waves from Y-type LB films having an even number of mono layers supports this argument. The degree of imperfection seemed to increase as the number of layers increased. The second-order nonlinear optical properties of spin-cast films of these polymers were also measured. The largest second harmonic coefficient of the poled P[DRIMA-MI] film coated on a glass plate was 19 pm/V.

• Asian-Australasian Journal of Animal Sciences
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• v.10 no.2
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• pp.185-191
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• 1997

This experiment was conducted to determine the effects of a low-protein diet supplemented with DL-methionine plus L-cystine (Met + Cys) on the growth performance and fat accumulation of female broiler chicks during the growing period (3-6 wks old). A low-protein diet (17% CP; 3,200 ME kcal/kg) was supplemented with Met + Cys (1.1 : 1.0) at levels 0.75, 0.94, 1.25, 1.31 or 1.50% of diet, respectively. Another diet with 21% CP and 3,200 ME kcal/kg served as the control group. All essential amino acids were adjusted to meet the National Research Council (1984) requirement for chicks. Feed and water were given ad libitum. Body weight of the chicks fed the low-CP diets supplemented with Met + Cys were heavier than those of the control birds. Feed conversion ratio and feed intakes were not significantly different between and among the treatment groups. Similary, abdominal fat content was not significantly different among the various treatments except that of the chicks fed the low CP diet with 1.25% Met + Cys which was higher than that of the control group. Fatty acid synthetase (FAS), acetyl-CoA carboxylase (ACC) activities and carcass protein content were not influenced by dietary treatments. Carcass fat content was lowest in chicks fed low CP diet with 0.75% Met + Cys and highest in the group that received 1.50% Met + Cys supplementation. Liver triglyceride increased as Met + Cys supplementation level increased. Various lipid fraction concentrations (cholesterol ester, free cholesterol, and phospholipid) in the serum went up as Met + Cys increased up to 1.25% after which it levelled off. Results of this experiment suggest that it is possible to reduce dietary protein level from 21% to 17% for growing broiler chicks by the supplementation of Met + Cys when other EAA were sufficient.

• 한국생물공학회:학술대회논문집
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• 2000.04a
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• pp.153-156
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• 2000

Xylan, the major hemicellulose component of many plants, occurs naturally in a partially acetylated form and lignin, the most resistant component in plant cell wall degradation, is also attached to ${\beta}-1,4-linked-D-xylose$ backbone through the ester linkage. Esterases are required to release the esterified substituent and acetyl esterases are important in the complete degradation of acetylated polysaccharides, like pectins and xylans. The gene(Axe) encoding acetyl xylan estarase(AXE) was isolated from genomic ${\lambda}$ library from Aspergillus ficuum. Nucleotide sequencing of the Axe gene indicated that the gene was separated with two intervening sequences and the amino acid sequence comparison revealed that it was closely related to that from A. awamori with the 92 % indentity. Heterologous expression of AXE was conducted by using YEp352 and Saccharomyces cerevisae 2805 as a vector and host expression system, respectively. The Axe gene was placed between GAL1 promoter and GAL7 terminator and then this recombinant vector was used to transform S. cerevisiae 2805 strain. Culture filtrate of the transformed yeast was assayed for the presence of AXE activity by spectrophotometry and, comparing with the host strain, four to five times of enzyme activity was detected in culture filtrate of transformed yeast.

• Asian-Australasian Journal of Animal Sciences
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• v.29 no.11
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• pp.1576-1584
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• 2016

Acetyl xylan esterase (AXE), which hydrolyzes the ester linkages of the naturally acetylated xylan and thus known to have an important role for hemicellulose degradation, was isolated from the anaerobic rumen fungus Neocallimastix frontatlis PMA02, heterologously expressed in Escherichi coli (E.coli) and characterized. The full-length cDNA encoding NfAXE1 was 1,494 bp, of which 978 bp constituted an open reading frame. The estimated molecular weight of NfAXE1 was 36.5 kDa with 326 amino acid residues, and the calculated isoelectric point was 4.54. The secondary protein structure was predicted to consist of nine ${\alpha}$-helixes and 12 ${\beta}$-strands. The enzyme expressed in E.coli had the highest activity at $40^{\circ}C$ and pH 8. The purified recombinant NfAXE1 had a specific activity of 100.1 U/mg when p-nitrophenyl acetate (p-NA) was used as a substrate at $40^{\circ}C$, optimum temperature. The amount of liberated acetic acids were the highest and the lowest when p-NA and acetylated birchwood xylan were used as substrates, respectively. The amount of xylose released from acetylated birchwod xylan was increased by 1.4 fold when NfAXE1 was mixed with xylanase in a reaction cocktail, implying a synergistic effect of NfAXE1 with xylanase on hemicellulose degradation.