• Journal of Sensor Science and Technology
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• v.6 no.3
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• pp.214-220
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• 1997

A thin film optical waveguide sensor has been developed to measure and analyze quantitatively some inherent optical properties of biochemical substances. In this paper, two different kinds of thickness of thin film waveguide were prepared by RF sputtering of Corning-7059 glass(n = 1.588 at ${\lambda}=\;514nm$, Ar laser) on Pyrex glass substrates. We made a sensing membrane coated on the thin film waveguide with the poly(vinyl chloride-co-vinyl acetate-co-vinyl alcohol) (91 : 3 : 6) copolymer membrane based on $H^{+}$-selective chromoionophore and $K^{+}$-selective neutral ionophore and then proposed the thin film opptical waveguide ion sensor which can select a potassium ion. This sensor based ell the absorbance change by utilizing chromoionophore and neutral ionophore, which changes their absorption spectrum in the UV-vis region upon complexation of the corresponding ionic species, have been reported. The sensitivity dependence of the proposed sensor on interaction length, waveguide thickness, and content of a chromoionophore was investigated. This sensor has the measurement range of $10^{-6}M{\sim}1M$ for $K^{+}$ concentration and 90% response time of duration within 1 min. Also, our thin film optical waveguide sensor using the evanescent field was investigated as compared with conventional transmission sensor or optode sensor by the optical fiber. The sensitivity of thin-film waveguide $K^{+}$ sensor is higher than that of the conventional transmission sensor. The proposed sensor is expected to be useful to biochemical, medical, environmental inspection and so on.

• Journal of Life Science
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• v.21 no.5
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• pp.761-765
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• 2011

Salt stability of enzymes is a crucial practical factor in the food industry. Previously, leucine aminopeptidase (LAP) was purified from Bacillus sp. N2. Here, we present the salt effect of LAP using synthetic substrates. LAP had a hydrolytic activity for L-leucine-${\rho}$-nitroanilide in high concentrations of NaCl (up to 4 M), but not for other neutral salts (LiBr, LiCl, NaBr, KBr, and KCl). It hydrolyzed various synthetic di-peptide substrates with hydrophobic and hydrophilic amino acids at the C-terminal Xaa region, in the presence of 0-4 M NaCl. The result indicated that the hydrolytic action of LAP is not dependent on the hydrophobicity of the amino acid side chain at the scissile bond of the substrate. Remarkably, the hydrolytic activity of LAP was 1-3 folds higher than those of other LAPs and aminopeptidases in 4.5 M NaCl, suggesting that NaCl-tolerant LAP might be used in the food industry as cheese and anchovy sauce.

• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.4
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• pp.587-594
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• 2010

To develop commercially available food protein hydrolysates, the effects of different types of enzymes and substrates on bitterness and solubility of partially hydrolyzed food proteins were investigated. Four types of proteins (casein, isolated soy protein (ISP), wheat gluten, and gelatin) and five types of proteolytic enzymes (a microbial alkaline protease (alcalase), a microbial neutral protease (neutrase), papain, bromelain, trypsin) were used. To profile the pattern of hydrolysis, the degree of hydrolysis (DH) were monitored during 180 min of reaction time by pH-stat method. Casein showed the highest susceptibility to hydrolysis for all five proteases compared to those of ISP, gluten, and gelatin. In addition, the bitter intensity and solubility (nitrogen soluble index, NSI) of each protein hydrolysate were compared at DH 10%. Bitterness and solubility of protein hydrolysates were highly affected by DH and the types of enzymes and substrates. At DH=10%, casein hydrolysate by trypsin, ISP and gluten hydrolysates by either bromelain or neutrase, and gelatin hydrolysates by the five proteases tested in this study were highly soluble and less bitter.

• Journal of Microbiology and Biotechnology
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• v.18 no.3
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• pp.410-416
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• 2008

The gene SfXyn10, which encodes a protease-resistant xylanase, was isolated using colony PCR screening from a genomic library of a feather-degrading bacterial strain Streptomyces fradiae var. k11. The full-length gene consists of 1,437bp and encodes 479 amino acids, which includes 41 residues of a putative signal peptide at its N terminus. The amino acid sequence shares the highest similarity (80%) to the endo-1,4-${\beta}$-xylanase from Streptomyces coelicolor A3, which belongs to the glycoside hydrolase family 10. The gene fragment encoding the mature xylanase was expressed in Escherichia coli BL21 (DE3). The recombinant protein was purified to homogeneity by acetone precipitation and anion-exchange chromatography, and subsequently characterized. The optimal pH and temperature for the purified recombinant enzyme were 7.8 and $60^{\circ}C$, respectively. The enzyme showed stability over a pH range of 4.0-10.0. The kinetic values on oat spelt xylan and birchwood xylan substrates were also determined. The enzyme activity was enhanced by $Fe^{2+}$ and strongly inhibited by $Hg^{2+}$ and SDS. The enzyme also showed resistance to neutral and alkaline proteases. Therefore, these characteristics suggest that SfXyn10 could be an important candidate for protease-resistant mechanistic research and has potential applications in the food industry, cotton scouring, and improving animal nutrition.

• Journal of Microbiology and Biotechnology
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• v.21 no.6
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• pp.617-626
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• 2011

Transglutaminase from Streptomyces mobaraensis is an enzyme of unknown function that cross-links proteins to high molecular weight aggregates. Previously, we characterized two intrinsic transglutaminase substrates with inactivating activities against subtilisin and dispase. This report now describes a novel substrate that inhibits papain, bromelain, and trypsin. Papain was the most sensitive protease; thus, the protein was designated Streptomyces papain inhibitor (SPI). To avoid transglutaminase-mediated glutamine deamidation during culture, SPI was produced by Streptomyces mobaraensis at various growth temperatures. The best results were achieved by culturing for 30-50 h at $42^{\circ}C$, which yielded high SPI concentrations and negligibly small amounts of mature transglutaminase. Transglutaminasespecific biotinylation displayed largely unmodified glutamine and lysine residues. In contrast, purified SPI from the $28^{\circ}C$ culture lost the potential to be cross-linked, but exhibited higher inhibitory activity as indicated by a significantly lower $K_i$ (60 nM vs. 140 nM). Despite similarities in molecular mass (12 kDa) and high thermostability, SPI exhibits clear differences in comparison with all members of the wellknown family of Streptomyces subtilisin inhibitors. The neutral protein (pI of 7.3) shares sequence homology with a putative protein from Streptomyces lavendulae, whose conformation is most likely stabilized by two disulfide bridges. However, cysteine residues are not localized in the typical regions of subtilisin inhibitors. SPI and the formerly characterized dispase-inactivating substrate are unique proteins of distinct Streptomycetes such as Streptomyces mobaraensis. Along with the subtilisin inhibitory protein, they could play a crucial role in the defense of vulnerable protein layers that are solidified by transglutaminase.

• Proceedings of the Korea Technical Association of the Pulp and Paper Industry Conference
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• 2001.04a
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• pp.18-25
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• 2001

A new wood-degrading fungus Trichophyton rubrum LKY-7 secretes a high level of laccase in a glucose-peptone liquid medium. The production of laccase by the fungus was barely induced by 2,5-xylidine. The laccase has been purified to homogeneity through three chromatography steps in an overall yield of 40%. The molecular mass of the purified laccase was about 65 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified laccase had the distinct blue color and had basic spectroscopic features of a typical blue laccase: two absorption maxima at 278 and 610 nm and a shoulder at 338 nm. The N-terminus of the laccase has been sequenced, revealing high homology to laccases from wood-degrading white-rot fungi such as Ceriporiopsis subvermispora. The enzyme had a "low" redox potential (0.5 V vs normal hydrogen electrode), yet it was one of the most active laccases in oxidizing a series of representative substrates/mediators. Compared with other fungal laccases, the laccase has a very low Km value with ABTS [2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid] as a substrate and a very high Km value with violuric acid as a substrate. The laccase has the isoelectric point of 4.0. The laccase had very acidic optimal pH values (pH 3-4) while it was more stable at neutral pH than at acidic pH. The laccase oxidized hydroquinone faster than catechol and pyrogallol. The oxidation of tyrosine by the laccase was not detectable under the reaction conditions. The laccase was strongly inhibited by sodium azide and sodium fluoride. fluoride.

• Bulletin of the Korean Chemical Society
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• v.34 no.11
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• pp.3335-3339
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• 2013

Boron-doped ZnO (BZO) nanorods were grown on quartz substrates using hydrothermal synthesis, and the temperature-dependence of their photoluminescence (PL) was measured in order to investigate the origins of their PL properties. In the UV range, near-band-edge emission (NBE) was observed from 3.1 to 3.4 eV; this was attributed to various transitions including recombination of free excitons and their longitudinal optical (LO) phonon replicas, and donor-acceptor pair (DAP) recombination, depending on the local lattice configuration and the presence of defects. At a temperature of 12 K, the NBE produces seven peaks at 3.386, 3.368, 3.337, 3.296, 3.258, 3.184, and 3.106 eV. These peaks are, respectively, assigned to free excitons (FX), neutral-donor bound excitons ($D^{\circ}X$), and the first LO phonon replicas of $D^{\circ}X$, DAP, DAP-1LO, DAP-2LO, and DAP-3LO. The peak position of the FX and DAP were also fitted to Varshni's empirical formula for the variation in the band gap energy with temperature. The activation energy of FX was about ~70 meV, while that of DAP was about ~38 meV. We also discuss the low temperature PL near 2.251 eV, related to structural defects.

• Korean Journal of Metals and Materials
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• v.49 no.10
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• pp.818-822
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• 2011

ZnO nanorods were grown on Au-coated Si substrates by vapor phase transport (VPT) at the growth temperature of $600^{\circ}C$ using a mixture of zinc oxide and graphite powders as source material. Au thin films with the thickness of 5 nm were deposited by ion sputtering. Temperature-dependent photoluminescence (PL) was carried out to investigate the optical properties of the ZnO nanorods. Five peaks at 3.363, 3.327, 3.296, 3.228, and 3.143 eV, corresponding to the free exciton (FX), neutral donor bound exciton ($D^{\circ}X$), first order longitudinal optical phonon replica of free exciton (FX-1LO), FX-2LO, and FX-3LO emissions, were obtained at low-temperature (10 K). The intensity of these peaks decreased and their position was red shifted with the increase in the temperature. The FX emission peak energy of the ZnO nanorods exhibited an anomalous behavior (red-blue-red shift) with the increase in temperature. This is also known as an "S-shaped" emission shift. The thermal activation energy for the exciton with increasing temperature in the ZnO nanorods is found to be about 26.6 meV; the values of Varshni's empirical equation fitting parameters are = $5{\times}10^{-4}eV/K$, ${\beta}=350K$, and $E_g(0)=3.364eV$.

• Journal of Adhesion and Interface
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• v.1 no.1
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• pp.23-29
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• 2000

Surface modification of hydrophobic polymeric materials to be hydrophilic or to have specific functional groups is of great importance for a diversity of applications of the materials. In this study, polyethylene (PE) film surfaces were modified by vapor phase photografting of hydrophilic vinyl monomers with different functional groups. The functional monomers were introduced on PE films by introducing the monomers in vapor phase using a vapor phase photografting apparatus designed by our laboratory. Functional monomers used were acrylic acid (negatively chargeable), acrylamide and allylalcohol (neutral), and allylamine and N,N-dimethyl aminopropyl acryamide (positively charged). The functional monomer-grafted PE film surfaces were characterized by the measurement of water contact angles and the attenuated total reflectance Fourier-transform infrared spectroscopy. The vapor phase photografting seems to be effective means for introduction of various functional groups onto polymeric substrates.

• YAKHAK HOEJI
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• v.38 no.5
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• pp.530-543
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• 1994

To study the feasibility of transmucosal delivery of leucine enkephalin (Leu-Enk) and $[D-ala^2]$-leucine enkephalinamide (YAGFL), their degradation extents and pathways in various rabbit mucosa extracts were investigated by high performance liquid chromatography. The degradation of Leu-Enk and YAGFL was observed to follow the first-order kinetics. The degradation half-lives of Leu-Enk in the nasal, rectal and vaginal mucosal extracts were 1.62, 0.37 and 1.12 hrs and those of YAGFL were 30.55, 9.70 and 6.82 hrs, respectively, indicating Leu-Enk was degraded in a more extensive and rapid manner than YAGFL. But the mucosal and serosal extracts of the same mucosa showed the similar degradation rates for both pentapeptides. The degradation was most rapid in the neutral pH and increasing concentrations of substrates retarded the degradation rates. The maior hydrolytic fragments of Leu-Enk were Des-Tyr-Leu-Enk and tyrosine, indicating the enzymatic hydrolysis by aminopeptidases. However, the data also suggested endopeptidases such as dipeptidyl carboxypeptidase and dipeptidyl aminopeptidase could play some role in the degradation of Leu-Enk. On the other hand, the hydrolytic fragments of YAGFL in all the mucosa extracts were mainly Tyr-D-Ala-Gly and Phe-Leu-Amide, demonstrating the hydrolytic breakdown by endopeptidases. The degradation pathways were further explored by concomitantly determining the formation of smaller metabolites of primary hydrolytic fragments of Leu-Enk and YAGFL in the mucosa extracts.