• The Korean Journal of Food And Nutrition
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• v.11 no.5
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• pp.576-579
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• 1998

Water extract of mulberry tree barks(Morus alba Linne) was studied for its proteolytic activity. Protein content of the extract was 1.12mg/ml and its specific activity was 5.14U/ml. The enzyme was active on various proteins : the relative acitities were 100 for casein, 63 for albumin, 58 for collagen, 45 for hemoglobin and 36 gelatin, respectively. There suggested that the ability of the enzyme to hydrolyze meat was relatively high since those are major meat proteins. Optimum pH and temperature for proteolytic activity were : pH 6.0 and 6$0^{\circ}C$. And the enzyme was stable at the pH range of 6.0 to 7.0 and temperature between 50 and 8$0^{\circ}C$. Apparent proteolytic activities could support some scientific grounds of traditional application of mulberry tree barks to home cooking for meat tenderization.

• Journal of the Korean Society of Food Science and Nutrition
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• v.30 no.3
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• pp.410-414
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• 2001

A new bacteriocin produced by Bacillus licheniformis cy2 was partially purified and characterized. The bacteriocin named as BSCY2 was stable in the pH range of 2.5~9.5. BSCY2 was stable below 4$0^{\circ}C$ and it retained its antimicrobial activity during long tern storage at -2$0^{\circ}C$ and -7$0^{\circ}C$. BSCY2 was inactivated 15 min exposure to temperatures over 8$0^{\circ}C$ and lost 50% of its antimicrobial activity within 2 hr at 7$0^{\circ}C$. BSCY2 was inactivated by proteinase K treatment, which indicates its proteinous nature. Direct detection of the BSCY2 band showing antimicobial activity on Tricine-SDS-PAGE suggested an apparent molecular mass of about 6,500 dalton. These characterizatics of BSCY2 are considered as potential compounds for use in bioindustry.

• Journal of The Korean Astronomical Society
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• v.29 no.spc1
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• pp.321-322
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• 1996

Using the data on the occurrences of the Ho: and soft X-ray flares for the time interval of January 1, 1986-May :31, 1994, we have studied the middle term(30-300days) pericities of the solar flare production during the activity cycle 22. Power analysis of the time seies of daily H$\alpha$ flare index in the northern hemisphere shows prominent periodicities at 220, 120, 109, and 92 days(see Figures l(a) and l(b)), while in the southern hemisphere, those at 267, 213, 183, 167, and 107 days are apparent, though their peaks are not so distint as those in the northern hemisphere. Periodogram of daily soft X-ray flare index also reveal the periodicities at 279, 205, 164, 117, and 91 days in the northern hemisphere, and at 266, 220, 199, 162, 120, and 100 days in the southern hemisphere. Howeer, the 155-day periodicity reported for the earlier cycles, 19, 20, and 21, could not be confirmed in our analysis. to be submitted to Solar Physics; an extended abstract.

• Toxicological Research
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• v.18 no.3
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• pp.301-309
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• 2002

Licorice has been wed in clinical medicine for thousands of years. However it is only in recent times that we have been able to employ scientific methods to prove its efficacy and to give us a better understanding of its mechanism of action. One of important mechanisms for its efficacy is related to mineralocorticoid activity increased by glycyrrhizic acid, the active ingredient in licorice. Also the main undesirable side-effects of Licorice relate to is mineralocorticoid activity resulting in a state of apparent mineralocorticoid excess (AME). These therapeutic and undesirable effects are explained by the inhibition of 11-$\beta$-hydroxysteroid dehydrogenase (11-$\beta$-HSD) activity. Recently, the reduction of serum testosterone in men by licorice was reported which would have important health implications in the context of fertility and sexual dysfunction. Here, health implication of licorice were reviewed In term of its pharmacodynamic and toxicodynamic mechanism.

• Biotechnology and Bioprocess Engineering:BBE
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• v.5 no.1
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• pp.53-56
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• 2000

A thermostable esterase from the hyper thermophilic archaeon Sulfolobus solfataricus was partially purified 590-fold with $16.2\%$ recovery. The partially purified esterase had a specific activity of $29.5\;{\mu}mol\;min^{-1}mg^{-1}$ when the enzyme activity was determined using p-nitrophenyl butyrate as a substrate. The apparent molecular weight was about 100 kDa, while the optimum temperature and pH for esterase were $75^{\circ}C$ and 8.0, respectively. The enzyme showed high thermal stability and solvent tolerance in comparison to its mesophilic counterpart. The enzyme also showed chiral resolution activity for (S)-ibuprofen, indicating that S. solfataricus esterase can be used for the production of commercially important chiral drugs.

• Preventive Nutrition and Food Science
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• v.21 no.4
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• pp.338-347
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• 2016

The present study investigated the volatile compound, physicochemical, and antioxidant properties of beany flavor-removed soy protein isolate (SPI) hydrolyzates produced by combined high temperature pre-treatment and enzymatic hydrolysis. Without remarkable changes in amino acid composition, reductions of residual lipoxygenase activity and beany flavor-causing volatile compounds such as hexanol, hexanal, and pentanol in SPI were observed after combined heating and enzymatic treatments. The degree of hydrolysis, emulsion capacity and stability, 2,2-diphenyl-1-picrylhydrazyl radical scavenging activity, and superoxide radical scavenging activity of SPI were significantly increased, but the magnitudes of apparent viscosity, consistency index, and dynamic moduli (G', G") of SPI were significantly decreased after the combined heating and enzymatic treatments. Based on these results, it was suggested that the enzymatic hydrolysis in combination with high temperature pre-treatment may allow for the production of beany flavor-removed SPI hydrolyzates with superior emulsifying and antioxidant functionalities.

• Fisheries and Aquatic Sciences
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• v.3 no.3_4
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• pp.188-194
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• 2000

A protease purified from hepatopancreas of shrimp, Penaeus japonicus, had maximum activity at $70^{\circ}C$ and in neutral and alkaline pH ranges. Specific activity at optimum reaction condition of the protease was estimated to be approximately 12 U/mg/min. The protease was stable in neutral and alkaline pH ranges and activity was retained after heat treatment at $50^{\circ}C$ for 30 min. Apparent $K_m$ and $V_{max}$ value against casein substrate were estimated to be $0.29\%$ and $7.8see^{-1}$, respectively, and those against N-CBZ-L-tyrosine p-nitropheny1 ester (CBZ­Tyr-NE) were 0.38 mM and $2,400 see^{-1}$, respectively. The N-termina1 sequence of the protease showed high homology to the trypsin from same species and the proteases from shrimp. Myosin heavy chain (MHC) from shrimp tail meat was the most susceptible to the protease and actin/tropomyosin were degraded progressively during 4 hr incubation, but to a lesser degree than MHC.

• Biomedical Science Letters
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• v.8 no.4
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• pp.245-250
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• 2002

Fibrinolytic enzyme has been purified from the edible mushroom, Tricholoma sejunctum using DEAE-cellulose chromatography, Phenyl-Sepharose chromatography and Mono-S column chromatography. The apparent molecular mass of purified enzyme was estimated to be 17100 Da by SDS-polyacrylamide gel electrophoresis and 19000 Da by gel filtration, Indicating that it was a monomer. The N-terminal amino acid sequence of the enzyme was Ala-Thr-Tyr-Lys-Ile-X-Ser-Ala-Thr-His-Gln-X-X-Leu-Val. It has a pH optimum at pH 9.5, suggested that purified enzyme was a alkaline protease. The activity of purified enzyme was inhibited by EDTA and 1,10-phenanthroline, indicating that purified enzyme is a metalloprotease. The activity of purified enzyme was increased by Zn$^{2+}$ and Co$^{2+}$, however, the enzyme activity was totally inhibited by Hg$^{2+}$.

• Journal of Microbiology and Biotechnology
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• v.14 no.2
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• pp.317-323
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• 2004

This study was performed to investigate the antimicrobial effects of hetero-chitosans and their oligosaccharides against three Gram-negative bacteria and five Gram-positive bacteria. Nine classes of hetero-chitosan oligosaccharides consisted of partially deacetylated chitosans; 90％, 75％, and 50％ deacetylated chitosans. Based on molecular weight, they were prepared using an ultrafiltration membrane reactor system. Seventy-five percent deacetylated chitosan showed the highest antimicrobial acitivity as compared with the 90％ and 50％ deacetylated chitosan, and the activity was dependent on their molecular weights. It was apparent that the growth of Gram-negative bacteria is less inhibited in the presence of the heterochitosans and their oligosaccharides than Gram-positive bacteria. These results revealed that the antimicrobial effects of hetero-chitosans and their oligosaccharides depend on the degree of deacetylation, and their molecular weights.

• International Journal of Industrial Entomology and Biomaterials
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• v.27 no.2
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• pp.329-332
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• 2013

In present preliminary report, we showed the possibility of silk sericin (SS) in enzyme immobilization. SS beads were prepared and enzymes were immobilized on it. The specific activity of immobilized a-chymotrypsin retained more than 87% compared to the free enzyme. The immobilized a-chymotrypsin has better stability against ethanol especially those immobilized on SS beads coagulated in methanol. Immobilized trypsin and lipase had also comparable apparent activity compared to free enzyme. Our result indicates that SS could be a good candidate for enzyme immobilization support due to its hydrophilicity.