• Korean journal of food and cookery science
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• v.26 no.5
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• pp.530-536
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• 2010

This study was the tenderizing activity of fig and kiwifruit using meat cooking. Furthermore, the effects of various seasonings and flavor spices were investigated. The proteolytic activity of kiwifruit was 36,513 uM/g fruit, whereas that of fig was 24,131 uM/g fruit. The best amount of fruit for meat cooking was 3~5% for kiwifruit and 5% for fig among three different dilutions, 3%, 5% & 10%. The effect of fruit ratio showed that treatment with 'kiwifruit only' produced the best organoleptic results, and there was no significant difference between the kiwifruit and fig ratios, 3:0, 2:1, 1:1. The best marinating time for meat tenderizing by fig and kiwifruit was 6hr at $4^{\circ}C$. The best marinating temperature for meat tenderizing by fig and kiwifruit was $25^{\circ}C$ rather than $4^{\circ}C$. Fruit sauce containing basic seasonings such as soy sauce, sugar, oligosaccharides, and sesame oil had a pH of 4.64 for fig and 4.23 for kiwifruit. The addition of soy sauce, oligosaccharides, and rice wine decreased the proteolytic activity of the fruits. Fruit sauce containing basic seasonings, garlic, ginger, onion and scallion had a pH of 4.71 for fig and 4.43 for kiwifruit. Finely chopped garlic, finely chopped scallion, and pureed onion, finely chopped ginger, and pear juice, all increased the proteolytic activity of the fruits. There the fruit sauce containing seasonings and flavory spices for meat cooking improved the tenderness and preference in terms of sensory evaluation without undesirable taste or increased fruits.

• Journal of environmental and Sanitary engineering
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• v.15 no.1
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• pp.77-87
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• 2000

Several new ion exchange resins have been synthesized from chloromethyl styrene-l,4-divinylbenzine with 1%, 2%, 10% and 20%-crosslink and macrocyclic ligands of cryptand type by interpolymerization method. The adsorption characteristics and the pH, time, solvents and concentration dependence of the adsorption of metal ions by this resin were studied. The correlation between the separation characteristics of uranium and transition metal on the resins and the stability constants of complexes with macrocyclic ligands have been examined. The resins were very stable in both acidic and basic media and have good resistance to heat. The $UO_2^{2+}$ was not adsorbed on the resins below pH 3.0, but the power of adsorption of $UO_2^{2+}$ increased rapidly above pH 4.0. The optimum equilibrium time for adsorption of metallic ions was two hours and adsorptive power decreased in proportion to crosslink size of the resins and order of dielectric constants of solvents used and the selective sequence for metal cations was in the order of $UO_2^{2+}$, $Ni{2+}$ and $Nd{3+}$.

• Microbiology and Biotechnology Letters
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• v.37 no.4
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• pp.383-388
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• 2009

A strain YB914 was isolated from soil as a producer of the extracellular xylanase, which catalyzes the hydrolysis of oat spelt xylan. The strain YB914 was identified as Streptomyces sp. on the basis of its morphological, cultural and biochemical properties. The xylanase of culture filtrate was the most active at $55^{\circ}C$ and pH 5.5, and retained 80% of its maximum activity at the range of pH 4.5~7.0. In order to optimize the culture medium for xylanase production, ingredients of G.S.S medium were replaced by several carbohydrates. The carbohydrates such as oat spelt xylan, corn cob xylan, wheat bran and lactose increased the xylanase productivity of Streptomyces sp. YB914. However, xylanase production was greatly repressed by galactose or arabinose. The maximum xylanase productivity was reached to 48 U/mL in the modified medium containing 1% oat spelt xylan and 1.5% lactose.

• Microbiology and Biotechnology Letters
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• v.9 no.4
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• pp.213-218
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• 1981

The molecular weight of the purified $\beta$-galactosidase of Penicillium sp. was estimated to be 130000 by both Sephadex G-200 gel filtration and SDS-polyacrylamide del electrophoresis. The SDS-electrophoresis gave two protein bands corresponding to the two molecular weights of 130000 and 70000. These results indicated that the enzyme consisted of two probably identical subunits which had a molecular weight of 70000. The optimum pH of the enzyme activity was 4.7 and maximum activity appeared at 5$0^{\circ}C$. The stable pH range for the enzyme was from 4.5 to 7.0. The purified $\beta$-galactosidase had no metal ion requirement for its activity or stability. The enzyme activity was inhibited by C $u^{++}$(1mM)and galactose (100mM). The hydrolysis of lactose in 5% lactose solution, pasteurized milk and 10% skim milk solution were 69.5%, 88.7% and 72.6% after 4 hr incubation at 5$0^{\circ}C$, when 10 units of $\beta$-glucosidase were used per $m\ell$ of the substrate solutions.s.

• Fisheries and Aquatic Sciences
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• v.5 no.3
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• pp.145-149
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• 2002

The effects of pH, temperature and various inhibitors on the proteolytic activity of the cell lysate of Uronema marium were investigated using colorimetric and substrate gel electro­phoretic methods. The cell lysate of U. marinum showed proteolytic activity over a wide range of pH, and pH optima ranged from pH 5 to 7. The proteolytic activity was increased according to a rise of temperature but decreased at $40^{\circ}$. The proteolytic activity of the parasite lysate was significantly inhibited by protease inhibitors including trans-epoxysuccinyl -L-leucylamido-(4-guanidino) butane (E-64), pepstatin A, phenyl-methanesulfonyl fluoride(PMSF), and ethylenediamine-tetraacetic acid (EDTA). Preincubation of the lysate with E-64 showed the maximum inhibition of the caseionolytic activity. Four protease bands (152, 97, 67 and 40 kDa) were detected by gelatin SDS-PAGE. Significant inhibition of caseinolytic activity and complete abolition of a 152 kDa band in gelatin SDS-PAGE by EDTA indicated that the cell lysate of U. marinum had a metalloprotease Another three proteolytic bands were inhibited by E64, a cysteine protease inhibitor. Preincubation of the cell lysate with pepstatin or PMSF had no effects on the protease bands.

• Journal of Digital Convergence
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• v.15 no.6
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• pp.545-550
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• 2017

This study conducted an experiment to develop new raw ingredients for natural cosmetics by evaluating the efficacy of cosmetic products containing the extracts of Pleurotus eringii mushrooms grown without agricultural chemicals. To this end, purchased were Pleurotus eringii mushrooms grown without agricultural chemicals in South Gyeongsang province, South Korea in 2016; extraction was conductedwith 80% EeOH at room temperature after dry ing them. The study identified the excellent efficacy of the extracts after evaluating the antioxidant activity using the DPPH assay and ROS assay. According to the evaluation of he categories of moisture, oil, pH and pigment after the application of a cream-type facial mask pack containing 5% of the extracts, there were significant differences in the categories of moisture and oil on the T-zone area, and no statistically significant differences in the categories of oil change on the U-zone, pH and pigment. However as the extracts of Pleurotus eringii mushrooms had excellent efficacy in all categories compared to the control group, the efficacy of the extracts as a cosmetic raw ingredient could be identified. It is expected that this study may further contribute to developing more advanced raw ingredients, given the extract and cultivation conditions by concentration.

• Microbiology and Biotechnology Letters
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• v.33 no.3
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• pp.178-183
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• 2005

A strain WL-2 was isolated from soil as a producer of the extracellular xylanase, which catalyzes the hydrolysis of oat spelt xylan. The strain WL-2 was identified as Streptomyces sp. on the basis of its 16S rRNA sequence, morphology, cultural and physiological properties. The xylanase of culture filtrate was the most active at $60^{\circ}C$ and pH 6.0, and retained $90{\%}$ of its maximum activity at range of pH $4.5{\~}6.5$. In order to optimize the culture medium for xylanase production, ingredients of G.S.S medium were replaced by several carbohydrates. The carbohydrates such as ${\alpha}-cellulose$, oat spelt xylan and maltose increased dramatically the xylanase productivity of Streptomyces sp. WL-2. The maximum xylanase productivity was reached to 120 U/ml in the modified medium containing $1{\%}\;\alpha-cellulose$ and $1\%}$ maltose.

• Microbiology and Biotechnology Letters
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• v.45 no.1
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• pp.12-18
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• 2017

Microbial strains exhibiting proteolytic activity were isolated from kimchi, one of traditional fermented foods in Korea. Eight strains formed clear zones around their colonies when grown on TSA plates supplemented with skim milk. MBE/L865 exhibited 2.6-fold higher protease activity than that of control strain (Bacillus subtilis KCTC13112). MBE/L865 was identified as B. subtilis and deposited in the Korean Collection for Type Cultures under the accession number of KCCM43059. The optimum growth conditions for B. subtilis KCCM43059 were determined to be $37^{\circ}C$ and pH 8. The strain showed maximum protease activity ($429.37{\pm}18.65U/mg$ protein) at $60^{\circ}C$ and pH 6. Further, B. subtilis KCCM43059 had a higher salt (NaCl) tolerance than that of the control strain.

• Applied Biological Chemistry
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• v.43 no.3
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• pp.169-173
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• 2000

For the development of enzyme detergent capable of effectively washing at low temperature, a bacterium producing alkaline protease was isolated from soil samples, and properties of the enzyme were investigated. The selected strain was Gram negative, rod shape$(0.6{\sim}0.7{\times}1.3{\sim}2.6\;{\mu}m\;in\;size)$ and motile. It had the degradation activity of aesculin, gelatin and casein, and was catalase-positive. The cell wall components was meso-DAP, and G+C mole contents was 43.3%. From these results, the strain was identified as Acinetobacter sp. KN-27. The activity of alkaline protease by this strain peaked with 3,300 D.U/mL after 36 hours in the liquid culture at $40^{\circ}C$. The optimal pH and temperature of the enzyme were pH 9 and $60^{\circ}C$, respectively. Alkaline protease produced by Acinetobacter sp. KN-27 has shown two active bands on the electrophoresis of native gel.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.2
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• pp.240-245
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• 1993

The optimum pH and temperature for the purified extracellular enzyme activity were 8.0 and 37$^{\circ}C$, respectively. NaCl was required for the activation of the enzyme and optimum concentration was 0.5M. This enzyme activity was inhibited by HgC $l_2$, CoC $l_2$ and ZnC $l_2$ and stimulated by CaC $l_2$. The activity of enzyme was increased by L-cysteine and 2-mercaptoethanol, but decreased by ο-phenanthroline, $\rho$-CMB, EDTA and iodoacetate. The $K_{m}$ and $V_{max}$ values of extracellular enzyme appeared as 0.717% and 15.39U/mg, respectively.y.