• YAKHAK HOEJI
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• v.38 no.5
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• pp.488-495
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• 1994

To evaluate the feasibility of transmucosal delivery of leucine enkephalin (Leu-Enk) and its synthetic analog, $[D-Ala^2]$-leucine enkephalinamide (YAGFL), their physicochemical stabilities in aqueous buffered solutions were first investigated using a stability indicating high performance liquid chromatography. The degradation of Leu-Enk and YAGFL followed the pseudo-first-order kinetics. From the pH-rate profiles, it was found that the maximal stability of the two pentapeptides was at the pH of about 5.0. The shelf lives $(t_{90%})$ for the degradation of Leu-Enk and YAGFL at pH 5.0 and $40^{\circ}C$ were found to be 48.13 and 50.9 days, respectively. From the temperature dependence of the degradation, activation energies for Leu-Enk and YAGFL were calculated to be 13.61 and 13.47 kcal/mole, respectively. A higher ionic strength and a higher initial peptide concentration in buffered solution slowed the degradation of the two pentapeptides. The addition of 2-hydroxypropyl-${\beta}$-cyclodextrin into the peptide solution did not affect the stability significantly.

• Korean Journal of Environmental Agriculture
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• v.21 no.2
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• pp.130-135
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• 2002

Water-dispersible colloids are suspected to facilitate transport of contaminants to groundwater. This study evaluated some soil chemical properties in relation to the stability of colloids in soils of Jeju citrus orchards. Thirty surface soil samples were collected, and pH, organic matter content oxalate-extractable Al and Fe contents, and water-dispersible colloid content were measured. In soils of higher pH, water-dispersible colloid contents were higher. The stability of colloids was found to be significantly promoted at pH above 5$\sim$6. Since organic matter can act as a flocculant organic matter content significantly enhanced the colloid stability. In soils of less than 5% organic C, water-dispersible colloid content was expected to be significantly higher. In soils of higher oxalate-extractable Al and Fe contents, colloids remaining in suspension were lower. This indicated that amorphous oxides and hydroxides play important stabilizing roles in soil structure and can stabilize soil clay against dispersion. Therefore in soils of higher pH, lower organic matter, and lower amorphous clay minerals, the stability of water-dispersible colloids and the potential of colloid-mediated transport of organic chemicals to groundwater could be higher.

• Microbiology and Biotechnology Letters
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• v.2 no.3
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• pp.133-140
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• 1974

1) Two xylanase (designed as A and B) of Myriococcus albomyces were purified from an extract of wheat koji culture. Puriscation steps included first ammonium sulfate fractionation followed successively by SE-Sephadex column chromatgraphy. DEAE-Sephadex column chromatography and gel filtration on Sephadex G-100 repectively. 2) The optimum pH and pH stability for crude xylanse were found to be pH 5.0 and pH 4.0-7.0 respectively. 3) The optimium temperature was found to he 5$0^{\circ}C$ and for the thermal statbility of xylanase, the enryme incubated at $65^{\circ}C$ for 60min did not affect their stability. 4) The purised xylanase A and B were considered as liquefying xylanase and saccharogenic xylauase repectively. 5) The Bylanase A was most active at pH 4.0 and range of pH 3.0-8.0 at 3$0^{\circ}C$ for six hrs. The B was most active at pH 5.0 showing stability range of pH 4.0 to 8.5 at 3$0^{\circ}C$ for 6 hrs. incubation respectively. The Optimum temperature of xylanase A and B were found to be 7$0^{\circ}C$ and $65^{\circ}C$ for 60min repectively.

• Proceedings of the Korean Society of Precision Engineering Conference
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• 2009.06a
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• pp.1093-1094
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• 2009

• Microbiology and Biotechnology Letters
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• v.24 no.4
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• pp.393-398
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• 1996

In order to develop a lactic acid bacterial powder which can be used as a probiotic for human and animal, a lactic acid bacteria which has high resistance against low pH and ox-gall, and shows a good growth inhibition against E. coli, was isolated from an animal intestine and characterized. The isolated strain was identified as Enterococcus faecium. It had more than 90% of survival at low pH for 2 hours and almost 100% of survival in the presence of 0.3% ox-gall. When co-cultured with E. coli in MRS broth, all of the E. coli cells were killed within 24 hours. The final powdered product of the isolated strain was manufactured after a freeze drying process using an industrial media, and then checked its stability. Its storage stability was 80% for 11 months at 18$\circ$C.

• The Korean Journal of Mycology
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• v.13 no.2
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• pp.111-114
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• 1985

The production of lac case by the funguson various media was studied. The characteristics of the enzyme were also studied regarding to the optimum pH, stability, Km value, and inactivation. The maximum activity of laccase reached the 40 days of incubation and the barley straw extract appeared to be a strong inducer for laccase. The enzyme showed stability at wide range of pH with optimum pH of 6.6. Temperature stability of the enzyme was high. Laccase was not inactivated by the organic solvents used for the precipitation. The enzyme, how­ever, was completely inactivated by trichloroacetic acid and sodium azide.

• Journal of the Korean Ceramic Society
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• v.37 no.7
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• pp.721-725
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• 2000

In this study, the dispersion stability of nano-sized CeO2 particles, synthesized by hydrothermal method in aqueous was evaluated from observing the surface potential behavior of CeO2 particle synthesized by solid state reaction. The isoelectric point(IEP) of nano-sized CeO2 synthesized by hydrothermal synthesis was found to be pH 9 contrary to the isoelectric point of micro-sized CeO2 synthesized by solid state reaction at pH 6.7. IEP was shifted to pH 2.0 as the addition of D-3019 from 0.1 to 1.0 wt%. The surface potential of CeO2 particles synthesized by hydrothermal synthesis was reduced as the addition of B-1001 used as a binder without change of IEP because the absorption of B-1001 polymer on the CeO2 particles shifted the shear plane of CeO2 particles outward away from the surface. This surface potential behavior was well correlated with the dispersion stability of slurry.

• Textile Coloration and Finishing
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• v.30 no.4
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• pp.264-274
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• 2018

Immobilization of lysozyme on chitosan non-woven using glutaraldehyde(GA) was investigated. For this, 100 % chitosan non-woven was prepared as novel support for the enzyme immobilization. In addition, free lysozyme activity was examined depending on various pH and temperature by measuring time. Moreover, the optimum immobilization conditions depending on various pH, temperature, immobilization time and lysozyme concentration was evaluated. In addition, thermal stability and storage stability of immobilized lysozyme were measured. The characteristics of immobilized lysozyme was examined by FT-IR, surface morphology, and MTT assay. The results are follows: the optimal immobilization of lysozyme were pH 7.0, $25^{\circ}C$, lysozyme concentration 1.5 mg/ml, immobilization time 240 min. The immobilized lysozyme showed higher thermal stability than the free trypsin. The immobilized lysozyme activity was retained 80 % of its initial activity at $4^{\circ}C$ over 30 days of storage. The lysozyme was immobilized effectively on chitosan non-woven by observation of surface morphology.

• KSBB Journal
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• v.13 no.5
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• pp.599-605
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• 1998

Soybean peroxidase was extracted from soybean hulls and purified by ammonium sulfate precipitations (25% and 75% saturation), pl fractionation, and anionic exchange and gel filtration chromatographies (DEAE-Sephadex A-50 and Superose 12). Modlecular weight and pl value were estimated to be ca. 45 kD and 4.2, respectively. Purified soybean peroxidase had an RZ value of 0.43. Compared with horseradish peroxidase, it showed superior thermal and pH stability. Assuming the first-order kinetics, the thermal deactivation rate constant of soybean peroxidase at 80$^{\circ}C$ was about 8 times lower than that of horseradish peroxidase. Deactivation energy was calculated to be 69.3 kcal/mol. Soybean peroxidase showed about 10% higher H2O2 degradation capacity than horseradish peroxidase. Exploiting these advantages, the soybean peroxidase purified from the domestic soybean hull is expected to replace horseradish peroxidase in various applications.

• Korean Journal of Food Science and Technology
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• v.25 no.5
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• pp.407-410
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• 1993

Stability of the anthocyanin pigment isolated from 'Comet' radish was decreased with increase of pH from 1.0 to 8.0. The destruction rate of anthocyanin at early stage was faster at pH 1.0 than pH 2.0 and 3.0, increased with increase of storage temperature from $0^{\circ}C\;to\;40^{\circ}C$. Thus the pigment preservability at $0^{\circ}C\;and\;40^{\circ}C$ after 10 days was 92.5% and 48.1%, and the half life at $0^{\circ}C\;and\;40^{\circ}C$ was 94.9 and 12.1 days, respectively Pigment was decreased with increase of ascorbic acid content from 0.015g to 0.05g.