• Journal of Microbiology and Biotechnology
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• v.5 no.4
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• pp.200-205
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• 1995

Nutritional factors regulating the morphological differentiation and physiological differentiation of Streptomyces exfoliatus SMF13 on surface cultures were evaluated. S. exfoliatus SMF13 produced leupeptin and chymotrypsin-like protease (CTP) at the stage of substrate mycelium growth, and leupeptin-inactivating enzyme (LIE) and trypsin-like protease (TLP) at the stage of aerial mycelium growth. The activity of leupeptin and CTP was high in the region of active growing substrate mycelium, whereas the activity of LIE and TLP was high in the region of aerial mycelium or spores. The differentiations were induced in glucose-limited conditions or by the addition of glucose anti-metabolite (methyl $\alpha$-glucopyranoside), but repressed by high concentrations of glucose or casamino acids. Morphological differentiation (formation of aerial mycelia and spores) was closely related with physiological differentiation (formation of brown-pigment, LIE and TLP). The local distribution of leupeptin, CTP, LIE, and TLP in a developing colony showed that colony development correlated with the production and functions of the compounds: CTP is essential for providing a nitrogen source for mycelium growth: leupeptin regulates TLP activity: LIE inactivates leupeptin: TLP hydrolyzes nongrowing mycelium.

• Journal of Microbiology and Biotechnology
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• v.18 no.5
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• pp.990-996
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• 2008

In a previous study, we found an antifungal effect on human pathogenic fungi by the cell-penetrating peptide Tat (47-58) derived from HIV-1. Tat (47-58) immediately entered into the fungal nucleus and affected some physiological changes on the intracellular condition. In this study, Tat (47-58) showed a broad spectrum of antibacterial activity against pathogenic bacteria including bacterial clinical isolates. To improve resistance against proteases for use in vivo, we synthesized an analog of Tat (47-58) by substituting the L-amino acid for the D-amino acid. The D-enantiomer of Tat (47-58) also exhibited a broad spectrum of antibacterial activity at almost the same level of L-Tat (47-58) concentration. Unlike L-Tat (47-58), D-Tat (47-58) showed a significant proteolytic resistance against all proteases tested and antimicrobial activities in the presence of trypsin. Moreover, D-Tat (47-58) inhibited MRSA infection in human HeLa cells whereas L-Tat (47-58) partially allowed MRSA infection, and the results were due to the proteolytic resistance of D-Tat (47-58).

• Microbiology and Biotechnology Letters
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• v.8 no.2
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• pp.113-117
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• 1980

The effects of divalant metal ions on the ATPase activity were studied by using my of ibrillar protein of rabbit (Chin-Chilla species) fed with vegetable oils. The results obtained were as follows : 1. The ATPase activity in myofibrillar protein of the is not significant to Rabbit exhibited a common biohapsic respnse, such as the ATPase activity is high at a lower ionic strength and low at a higher ionic strength. 2. The effect of EDTA on the ATPase activity of Myofibrillar protein extracted from Rabbit fed vegetable oils was tested by using various concentrations. The ATPase activity was inhibited from 0.2mM and over concentration of EDTA. 3. The ATPase activity in Myofibrillar protein was decreased remarkably in 0.2mM and over concentration for $Mg^{2+}$, and in 1.0mM and over concentration for $Ca^{2+}$. 4. in vitro, the digestibilities in A, B, C and D groups of Rabbit muscle treated with Papsin and Trypsin for 30 minutes at 36$^{\circ}C$ water bath were 71.66％, 73.87％ ； 70.62％, 77.93％ ； 67.93％, 76.52％ ； and 86.79％, 90.22%, respectively.y.

• Food Science and Preservation
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• v.30 no.6
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• pp.999-1011
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• 2023

This study investigated the anti-inflammatory, trypsin activity, and antioxidant effects of 11 kinds of plant extracts to discover materials for developing optimal mixtures that improve inflammation and help digestion. Ziziphus jujuba Mill. (ZJ), Leonurus japonicus Houtt. (LJ), Scutellaria baicalensis (SB), Platycodon grandiflorum, and Aster scaber extracts had excellent anti-inflammatory effects by reducing excessive nitric oxide (NO) and tumor necrosis factor-α content in lipopolysaccharide (LPS)-stimulated RAW264.7 macrophages. The malt (MA), Pyrus pyrifolia Nakai (PP), Raphanus sativus L., Platycodon grandiflorum extracts among the 11 kinds of plant extracts had high trypsin activity. The antioxidant activity of the plant extracts was examined by the DPPH radical scavenging activity, and the SB, PE, JU, and MA extracts had high antioxidant activity. Therefore, PP, MA, ZJ, LJ, and SB were selected to develop optimal mixtures that improve inflammation and help digestion. The extract of plant mixture containing PP, MA, ZJ, LJ, and SB in the ratio 1:1:2:1:2 (w/w) significantly inhibited NO production than the extract of PP, MA, ZJ, LJ, and SB, respectively, in LPS-stimulated RAW 264.7 macrophages. The DPPH radical scavenging activity of the mixture extract was significantly higher than the extract of PP, MA, ZJ, and LJ, respectively.

• Microbiology and Biotechnology Letters
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• v.36 no.1
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• pp.28-33
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• 2008

The expression vector (pWHM3-TR1R2) for sprT gene encoding Streptomyces griseus trypsin (SGT) followed by two regulatory genes, sgtR1 and sgtR2, was introduced into Streptomyces lividans TK24 and Streptomyces griseus IFO 13350. Various media with different compositions were used to maximize the productivity of SGT in the recombinant trains. he SGT productivity was best when the transformant of S. lividans TK24 was cultivated in R2YE medium (0.74 unit/mL) at 5 days of cultivation. C5/L (0.66 unit/mL) medium also gave a good productivity, but Livid (0.08 unit/mL) and NDSK (0.06 unit/mL) yielded poor productivities. S. griseus IFO 13350/pWHM3-TR1R2 produced SGT by 1.518 unit/mL (C5/L), 1.284unit/mL (R2YE),0.932 unit/mL (NDSK), and 0.295 unit/mL (Livid) at 7 days of cultivation, which was much higher than those from S. lividans TK24/TR1R2. The SGT protein was purified from the culture broth of S. griseus IFO 13350/pWHM3-TR1R2 in C5/L to homogeneity via ammonium sulfate fractionation, and CM-sepharose and SP-sepharose column chromatographies. The specific activity of purified SGT was 69,252 unit/mg, and the final purification fold and recovery yield were 6.5 and 1.4%, respectively.

• Journal of the Korean Society of Food Science and Nutrition
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• v.21 no.3
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• pp.255-262
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• 1992

In vitro digestibility of filefish, protein was substantially decreased by fiber constituents in the follow-ing order : pectin (9.97%), gum karaya (7.03%), sodium alginate (6.12%),and cellulose (1.52%). The order of reduction by fibrous residues from vegetables ranked as follows : sea tangle (12.36%), Ro-maine lettuce (11.12%), perillar leaf (8.96%), and green pepper (5.15%). The inhibitory effect of the dietary fibers towards filefish protein digestion, expressed as soybean trypsin inhibitor equivalents, in-creased with added levels, but the inhibition differed with the sources of dietary fibers. Sea tangle and sodium alginate were most active in decreasing the concentration of essential amino acid from filefish protein hydrolysis. Sodium alginate exerted an inhibitory effect on the activity of trypsin, but the other fiber constituents did not have an inhibitory potency on trypsin and bacterial pretense (Streptomyces griceus). Results supported that dietary fiber components may reduce protein digestibility through the interaction of dietary fiber components with filefish protein.

• Journal of Microbiology and Biotechnology
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• v.8 no.4
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• pp.333-340
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• 1998

Streptomyces griseus trypsin (SGT) is an extracellular proteinase produced by S. griseus. The sprT gene, which encodes premature SGT protein, was cloned into the plasmid pWHM3, a Streptomyces-E. coli shuttle vector. When the recombinant plasmid was introduced into Streptomyces lividans TK24, two proteins with molecular weights of 28 kDa and 42 kDa were detected. The 28-kDa protein was a SGT protein while the larger 42-kDa protein is thought to have been a premature form of the SGT protein. The SGT protein was purified to homogeneity via ammonium sulfate fractionation and many column chromatographies, including CM -sepharose chromatography, Mono-S chromatography, and Superose-12 chromatography, from the culture broth of S. lividans TK24 harboring the sprT gene. The N-terminal amino acid sequence, isoelectric points, and stabilities at various conditions of the SGT proteins purified from the Pronase and transformant were almost identical. The amount of the expressed SGT in S. lividans TK 24 was determined to be 5 times more than that of S. griseus based on the enzymatic activity against artificial substrate.

• Applied Chemistry for Engineering
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• v.5 no.2
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• pp.321-326
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• 1994

The water-soluble polyphosphazene possessing ether side groups was exposed to ${\gamma}-rays$ to prepare hydrogens with good water-swellability. The physical strength of these hydrogels could be controlled by irradiation dose of ${\gamma}-rays$. Trypsin and water-soluble polyphosphazene were irradiated together by ${\gamma}-rays$ for entrapment of enzymes into hydrogel networks. The activities of immobilized trypsin were examined spectrophotometrically after the reaction with N-${\alpha}$-benzoyl-1-arginine-p-nitroanilide in phosphate buffer. The immobilized trypsin was found to have good activity yield and suability after at least 500 hours.

• Food Science and Biotechnology
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• v.18 no.3
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• pp.706-711
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• 2009

Lysozyme was treated with digestive enzymes and the production of interleukin 8 (IL-8) was measured in Caco-2 cell with the peptides from lysozyme upon stimulating with lipopolysaccharide (LPS) to investigate the overall anti-inflammatory activity of lysozyme when it is in digestive tracts. Lysozyme reduced IL-8 production, and the peptides from pepsin hydrolysis of lysozyme had the similar effect. The products of trypsin digestion of lysozyme had no effect on the reduction of IL-8 production while those of pepsin-trypsin hydrolysis did. The effectiveness of lowering IL-8 production was not different by time of the peptide addition. When Caco-2 cells were pre-incubated with peptides for 24 hr, the reduction effects were observed from the peptides from pepsin hydrolysis, indicating that some of the peptides are still remaining in the cells. Therefore, it can be concluded that the IL-8 reduction effect of lysozyme against LPS still remained even after the pepsin and trypsin hydrolysis.

• Korean Journal of Food Science and Technology
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• v.6 no.2
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• pp.79-85
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• 1974

To obtain further information concerning the nature myofibrillar proteins in a food system, an investigation has been conducted to compare the change in the biochemical property of the myofibril with the changes in the morphological structure of the myofibril. When myofibrils were prepared with 0.16 M KCl-0.04 M Tris-HCl, the band pattern was clear and distinct. There was a uniform thickening of A-band, a sharp appearence of Z-lines and a wide I-band. The band pattern of myofibrils was changed as the composition of extraction solution was changed. Also the ATPase activity of myofibril changed as the length of sarcomere changed. When myofibrils were treated with a low concentration of trypsin, myofibrils turned in the contracted state. With the progress of prolonged trypsin treatment, most of myofibrils exhibited a pattern of alternating light and dark bands, supercontracted pattern. Although myofibrils exhibited a supercontracted band pattern, the ATPase activity of myofibril continued to increase with the progress of trypsin treatment. An assumption was made that tropomyosin may be located in Z-line and that troponin-tropomyosin complex can inhibit the ATPase activity of myofibrils through the structural alternation of myofibril.