• Journal of Microbiology
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• v.44 no.2
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• pp.243-247
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• 2006

Mycobacterium sp. strain JC1 was capable of growth on benzylamine as a sole source of carbon and energy. The primary deamination of benzylamine was mediated by an inducible amine oxidase, which can also oxidize tyramine, histamine, and dopamine. Inhibitor study identified this enzyme as a copper-containing amine oxidase sensitive to semicarbazide.

• Bulletin of the Korean Chemical Society
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• v.30 no.11
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• pp.2773-2776
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• 2009

• Applied Chemistry for Engineering
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• v.8 no.3
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• pp.365-373
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• 1997

Chitosan oligomer having aldehyde group at reducing end was prepared by oxidative-deamination reaction of chitosan by using sodium nitrite, and the resulting aldehyde group was redeced to 2,5-anhydro-D-mannitol group. The obtained chitosan oligomer showed an average degree of polymerization(DP) 2 by GPC analysis. It was highly soluble in lipophilic solvents. N,N-diacyl, O-acyl chitosan oligomer was obtained trom the reaction between chitosan oligomer and acyl chloride under 4-dimethoxyaminopyridine catalyst. From DSC measurement, N,N-dilauroyl, O-lauroyl chitosan oligomer showed mesophase region, which was confirmed by polarizing microscope as thermotropic liquid crystalline state. X-ray diffraction pattern revealed that N,N-dilauroyl, O-lauroyl chitosan oligomer was highly crystalline, whereas chitosan oligomer was not.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.25 no.1
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• pp.6-22
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• 1999

Chitosan oligosaccharide having physiological activity, such as cell proliferation and wound healing, was prepared by NaNO$_2$ oxidation-NaBH$_4$ reduction from natural chitosan. After deamination by NaNO$_2$ oxidation, the reducing-end residue from NaBH$_4$ was converted to alditol unit, and the reduction was checked by MBTH reagent. The resulting chitosan oligosaccharide had a degree of polymeration of 2-6 from HPLC analysis. From moisture absorption test at relative humidity of 43% and 81%, the moisture absorption ability was 63% and 57%. Moisture retention ability at relative humidity of 43%, silica gel emvironment, was 98% and 97% respectively. Cell proliferation was showed In the range of 0.000032~0.01%, wound healing effect was also appeared in the concentration of 2% and 20%. Antioxidative effect ($SC_{50}$/) was 3213 ppm. Chitosan oligosaccharide was compatible with most of ingredients used in cosmetic products.

• Bulletin of the Korean Chemical Society
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• v.35 no.5
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• pp.1269-1274
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• 2014

Monoamine oxidases catalyze the oxidative deamination of dietary amines and amine neurotransmitters, and assist in maintaining the homeostasis of the amine neurotransmitters in the brain. Dysfunctions of these enzymes can cause neurological and behavioral disorders including Parkinson's and Alzheimer's diseases. To understand their physiological roles, efficient assay methods for monoamine oxidases are essential. Reviewed in this Perspective are the recent progress in the development of fluorescent probes for monoamine oxidases and their applications to enzyme assays in cells and tissues. It is evident that still there is strong need for a fluorescent probe with desirable substrate selectivity and photophysical properties to challenge the much unsolved issues associated with the enzymes and the diseases.

• Journal of Microbiology and Biotechnology
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• v.5 no.5
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• pp.305-308
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• 1995

From the plasmid library made from Sstl and San-digested genomic DNA of Streptomyces fradiae NRRL 2702, four positive clones were selected using an oligodeoxynucleotide probe from the N-terminal amino acid sequence of purified threonine dehydratase. The cloned gene for threonine dehydratase was a 2.0 kilo-base pair DNA fragment. The deduced amino acid sequence of PCR product (PCR245) was matched to that of the N-terminal part of threonine dehydratase from S. fradiae and this showed a high similarity to the threonine dehydratases of other organisms. This indicated that amino acid sequences of threonine dehydratases were highly conserved and the polypeptide product of the PCR245 was likely to be involved in the deamination of threonine.

• Journal of the Korean Society of Food Science and Nutrition
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• v.27 no.2
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• pp.305-312
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• 1998

Normal tensile strength in collagen fibrils is due to intermolecular and intramolecular crosslinks which are known to be altered in aging. Pyridinoline, a mature crosslink which is stable and nonreducible, is derived from two hydroxyallysine and one hydroxylysine residues of collagen fibrils. The excess formation of pyridinoline in collagen is associated with making the tissue stiffer, less soluble and less digestible by enzymes. Lysyl oxidase is the enzyme that initiates the biosynthesis or crosslinks in collagen by catalyzing the oxidative deamination of the lysyl and hydroxylysyl residues in these molecules, and its activity is inhibited by $\beta$-aminopropionitrile(BAPN). Our previous work demonstrated that the pyridinoline content of bone collagen significantly was increased during incubation for 5 weeks at 37$^{\circ}C$ invitro, but it was diecrased by the addition of ascorbic acdi(AsA). In this study, we clarified the specific action of AsA in aging process in vitro enzymatic reaction.

• Bulletin of the Korean Chemical Society
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• v.21 no.4
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• pp.379-382
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• 2000

The temperature dependence of the kinetic parameters of the aspartase-catalyzed reaction has been examined in the direction of deamination. The pK1values at 37$^{\circ}C$, 25$^{\circ}C$, 16$^{\circ}C$ and 7$^{\circ}C$ were 6.2 $\pm$ 0.1, 6.3 $\pm$ 0.1, $6.7{\pm}0.3$ and 6.9 $\pm$ 0.3, respectively. On the other hand, the pK2 values at 37$^{\circ}C$,25$^{\circ}C$, 16$^{\circ}C$ and 7$^{\circ}C$ were 8.1 $\pm0.2$, 8.3 $\pm$ 0.2, 8.2 $\pm$ 0.3 and 8.0 $\pm$ 0.2,respectively. The enthalpy of ionization, DHion, calculated from the slope of pK1, are 6.0 $\pm$ 0.3 kcal/mol. These results validate the prediction that aspartase requires a histidine residue for a general base, and a cysteine (or having a carboxyl functional group) for a general acid.

• Microbiology and Biotechnology Letters
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• v.31 no.1
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• pp.25-31
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• 2003

Delftia acidovorans 51-A isolated from river water degrades aniline. In order to clone genes involved in aniline degradation, transposon Tn5-B20 was inserted into the strain 51-A to generate a mutant strain 10-4-2 that cannot utilize aniline as a carbon source. The mutant strain was not an auxotroph but could not degrade aniline. Southern hybridization analysis indicated that the transposon was inserted into the mutant bacterial DNA as a single copy. Flanking DNA fragment of Tn5-B2O insertion was cloned and sequenced. DNA sequence analysis revealed three ORFs encoding TdnQ, TdnT, and TdnA 1 that arc responsible for catechol formation from aniline through oxidative deamination. The analysis also confirmed that Tn5-B2O was inserted at the immediate downstream of tdnA1. The result suggests that the transposon insertion behind tdirA1 disrupted the pathway of the catechol formation from aniline, resulting in the mutant phenotype, which cannot degrade aniline. A large plasmid over 100-kb in size was detected from D. acidovorans 51-A and Southern hybridization analysis with Tn5-B2O probe showed that the transposon was inserted on the plasmid named pTDN51. Our results indicated that the tdn genes on pTDN51 of D. acidovorans 51-A are involved in aniline degradation.

• Preventive Nutrition and Food Science
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• v.2 no.4
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• pp.354-359
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• 1997

Optimal cultivation conditions for the production of phenylalanine ammonia-lyase(PAL) from Rhodotorula aurantiaca K-505 were selected, and the kinetic parameters of the produced PAL were determined. The most suitable carbon and nitrogen sources were glucose and tryptone, respectively. The strain expressed PAL constituttively when using the optimized semi-complex media. High cell density culture could be critical for maximal production of PAl since the PAL ynthesis was growth associated. maximum PAL activity was observed at initial pH 6.0. although the ll growth was not markedly affected by temperature between 22 and 28$^{\circ}C$, the cells yielded the maximum PAL activity when cultivated at 22$^{\circ}C$. The maximum activity for deamination of L-phenylalnine to trans-cinnamic acid was observed around pH 8.8. The PAL activity gave the maximum at 45$^{\circ}C$, and greatly decreased at higher than 5$0^{\circ}C$. Activation energy({TEX}$E_{a}${/TEX}) calculated from Arrhenius equation was 6.28 kcal/mol in the range of 22$^{\circ}C$ to 4$0^{\circ}C$. A oolf plot showed that the enzyme reaction follows Michaelis-Menten equation, whose {TEX}$K_{M}${/TEX} and {TEX}$V_{max}${/TEX} values were 4.65$\times${TEX}$10^{-3}${/TEX} M and 0.89$\mu$ mol/mg-min respectively.