• Food Science and Preservation
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• v.3 no.2
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• pp.187-193
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• 1996

To investigate the antimicrobial activities and effect of grapefruit seed extract(GFSE) on the physiological function of microorganism, antimicrobial activity, fatty acids of bacterial cell lipid and amino acids of bacterial cell protein were measured. The change of cell morphotype was observed by transmission electron microscope. GFSE was very stable on the wide range temperture and pH. The growth rate of E. coli and B. suvtilis were decreased above 40ppm GFSE There fore, minimum inhibitory concentration (MIC) of the E. coli and B. subtilis to GFSE were determined around 40ppm. In the change of fatty acids quantities, hexadecanoate was significantly decreased on the treatment compared with control in case of E. coli, whereas tridecanoate was not detected in case of B. subtilis. In the change of amino acids quantities, alanine, glutamic acid, glycine, lysine were decreased on the treatment compared with control in case of E. coli and B. subtilis Transmission electron microsgraphs(TEM) showed the microbial cells were destroyed by GFSE.

• Bulletin of the Korean Chemical Society
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• v.32 no.9
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• pp.3219-3222
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• 2011

Three types of ${\beta}$-ketoacyl acyl carrier protein synthase (KAS) are important for overcoming the bacterial resistance problem. Recently, we reported the discovery of a antimicrobial flavonoid, YKAF01 (3,6-dihydroxyflavone), which exhibits antibacterial activity against Gram-positive bacteria through inhibition of ${\beta}$-ketoacyl acyl carrier protein synthase III (KAS III). In this report, we suggested that YKAF01 can be an inhibitor ${\beta}$-ketoacyl acyl carrier protein synthase I (KAS I) with dual inhibitory activity for KAS I as well as KAS III. KAS I is related to the elongation of unsaturated fatty acids in bacterial fatty acid synthesis and can be a good therapeutic target of designing novel antibiotics. We performed docking study of Escherichia coli KAS I (ecKAS I) and YKAF01, and determined their binding model. YKAF01 binds to KAS I with high binding affinity ($2.12{\times}10^6$) and exhibited an antimicrobial activity against the multidrug-resistant E. coli with minimal inhibitory concentration (MIC) value of 512 ${\mu}g$/mL. Further optimization of this compound will be carried out to improve its antimicrobial activity and membrane permeability against bacterial cell membrane.

• Journal of Microbiology and Biotechnology
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• v.25 no.7
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• pp.1007-1014
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• 2015

Plectasin, the first defensin extracted from a fungus (the saprophytic ascomycete Pseudoplectania nigrella), is attractive as a prospective antimicrobial agent. The purpose of this study was to establish a bacterium-based production system and evaluate the antimicrobial activity of the resulting plectasin. A gene encoding plectasin, with the codon preference of Escherichia coli, was optimized based on its amino acid sequence, synthesized using genesplicing with overlap extension PCR, and inserted into the expression vector pGEX-4T-1. The fusion protein was expressed in the soluble fraction of E. coli and purified using glutathione Stransferase affinity chromatography. Plectasin was cleaved from the fusion protein with thrombin and purified by ultrafiltration. The purified plectasin showed strong, concentrationdependent antimicrobial activity against gram-positive bacteria, including antibiotic-resistant bacteria, especially penicillin-resistant Enterococcus faecium. This antimicrobial activity was equal to chemically synthesized plectasin and was maintained over a wide range of pH and temperatures. This soluble recombinant expression system in E. coli is effective for producing plectasin at a relatively lower cost, and higher purity and efficiency than prior systems, and might provide a foundation for developing a large-scale production system. Overall, plectasin shows potential as a novel, high-performance, and safe antibiotic for the treatment of refractory diseases caused by drug-resistant bacterial strains.

• Animal Bioscience
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• v.34 no.9
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• pp.1525-1531
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• 2021

Objective: The objective of this study was to evaluate the antimicrobial effects of fermented Maillard reaction products made by milk proteins (FMRPs) on Clostridium perfringens (C. perfringens), and to elucidate antimicrobial modes of FMRPs on the bacteria, using physiological and morphological analyses. Methods: Antimicrobial effects of FMRPs (whey protein plus galactose fermented by Lactobacillus rhamnosus [L. rhamnosus] 4B15 [Gal-4B15] or Lactobacillus gasseri 4M13 [Gal-4M13], and whey protein plus glucose fermented by L. rhamnosus 4B15 [Glc-4B15] or L. gasseri 4M13 [Glc-4M13]) on C. perfringens were tested by examining growth responses of the pathogen. Iron chelation activity analysis, propidium iodide uptake assay, and morphological analysis with field emission scanning electron microscope (FE-SEM) were conducted to elucidate the modes of antimicrobial activities of FMRPs. Results: When C. perfringens were exposed to the FMRPs, C. perfringens cell counts were decreased (p<0.05) by the all tested FMRPs; iron chelation activities by FMRPs, except for Glc-4M13. Propidium iodide uptake assay indicate that bacterial cellular damage increased in all FMRPs-treated C. perfringens, and it was observed by FE-SEM. Conclusion: These results indicate that the FMRPs can destroy C. perfringens by iron chelation and cell membrane damage. Thus, it could be used in dairy products, and controlling intestinal C. perfringens.

• Korean Journal of Food Science and Technology
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• v.31 no.2
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• pp.540-546
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• 1999

The purpose of this study was to investigate the antimicrobial effects and characteristics of protamine extracted from spermary of tuna. The result of amino acids analysis showed that the contents of arginine were 46%. It was 10% lower when compared to standard protamine (SP: Asama kasei LTD, Japan). Also, there were significant difference in the contents of proline adn glycine. The average molecular weights of main protein in TP were 13,400 Da, whereas those in SP were 11,300 Da and 2,600 Da. To increase antimicrobial activities of TP, pepsin or trypsin was treated at $37^{\circ}C$. After TP was hydrolyzed with pepsin (pepsin hydrolyzed protamine: PHP) for 4hrs, the average molecular weights of the main protein were 11,300 Da and 3,900 Da, and the antimicrobial activities were significantly increased compared to TP. After TP was hydrolyzed with trypsin (trypsin hydrolyzed protamine: THP) for more than 10 min, the average molecular weights of the main protein were below 2,500 Da. PHP had higher antimicrobial effects on some gram positive bacteria (Staphylococcus aureus, Lactobacillus helveticus, Lactobacillus plantarum) than SP. However, THP had no antimicrobial activities. When TP was hydrolyzed with pepsin (PHP), its antimicrobial activities increased in the same level with those of SP, and this increase might be resulted rather from the changes of molecular weights of the main protein than from the contents of arginine in protamine.

• Journal of the Korean Society of Clothing and Textiles
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• v.35 no.4
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• pp.466-475
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• 2011

The dyeing properties of protein fiber with pine needles colorants were studied through an investigation of the effect of dyeing conditions such as dye concentration, dyeing temperatures and time on dye uptakes, effect of mordants, and color change. In addition, the various colorfastness of dyed silk and wool fabrics were evaluated for practical use. The antimicrobial ability, ultraviolet-cut ability, and deodorant ability were also estimated. The dye uptake increased as the dyeing concentration increased and this enabled the obtainment of the Langmuir absorption isotherm. The dye uptake increased as the dyeing time and temperature increased. Pine needles colorants showed relatively good affinity to protein fiber and produced a yellow color. Post-mordanting was more effective than the pre-mordanting, and the dye uptake of fabrics improved by mordanting. Except for washing, the colorfastness of dyed fabrics showed a low rating. However, the colorfastness to light and the dry cleaning of fabrics mordanted with N.Cu, and the friction fastness of fabrics mordanted with Cu improved. The guide fabrics showed very good antimicrobial abilities of 99.9%; in addition, the ultraviolet-cut ability and deodorant ability improved in fabrics dyed with pine needles extracts.

• Journal of Microbiology and Biotechnology
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• v.20 no.2
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• pp.350-355
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• 2010

Among human antimicrobial peptides (hAMPs), DCD-1L has a broad spectrum of antimicrobial activity over a wide pH range and in high salt concentrations. It offers a promising alternative to conventional antibiotics. The 458-bp-long dermcidin cDNA was amplified by PCR using a human fetal cDNA library as a template. The 147-bp fragment of the MDCD-1L gene encoding an additional methionine residue was subcloned into the pTYB11 vector. Recombinant MDCD-1L was expressed as an intein fusion protein in E. coli, and then purified by affinity chromatography using chitin beads. A small peptide with a molecular mass of about 5 kDa was detected by tricine gel electrophoresis. The recombinant MDCD-1L peptide was purified from the gel and its amino acid sequence was determined by nanoLC-ESI-MS/MS analysis. The initiating amino acid, methionine, remained attached to the N-terminal region of recombinant MDCD-1L. Purified MDCD-1L showed antimicrobial activity against a Micrococcus luteus test strain.

• Korean Journal of Plant Resources
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• v.25 no.5
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• pp.543-549
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• 2012

To gather the basic data for increasing the utilization of Isatis tinctoria, we examined the effects of both antioxidative enzyme activity and antimicrobial activity from the extract of Isatis tinctoria. Ascorbate Peroxidase activities reveal that there is an decrease in order; ethanol extract from its stem (1601.7 Unit/mg protein), methanol extract from its leaf (1133.7 Unit/mg protein) and distilled water extract from its leaf (524.3 Unit/mg protein). Catalase activities reveal that there is an decrease in order; ethanol extract from its flower petal (177.1 Unit/mg protein), methanol extract from its leaf (120.8 Unit/mg protein) and distilled water extract from its flower petal (55.4 Unit/mg protein). Peroxidase activities reveal that there is an decrease in order; ethanol extract from its flower petal (27.1 Unit/mg protein), methanol extract from its flower petal (14.6 Unit/mg protein) and distilled water extract from its stem (10.4 Unit/mg protein). Superoxide dismutase activities reveal that there is an increase in order; distilled water extract from its root (90.8%), methanol extract from its flower petal (80.1%) and ethanol extract from its root (75.5%). Its flower extract showed a antimicrobial activity only against Vibrio parahaemolyticus, its root extract had only against Staphylococcus aureus, and its stem extract had against Bacillus subtilis, Escherichia coli and Staphylococcus aureus, regardless of solvents. Especially, distilled water extract from its leaf showed a high antimicrobial activity against both Bacillus subtilis and Escherichia coli and inhibition diameters against those were 30.0 and 24.0 mm, respectively.

• Journal of Microbiology and Biotechnology
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• v.14 no.6
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• pp.1303-1309
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• 2004

In order to extend shelf-life of the packaged or coated foods, an antibacterial edible film was developed. Antimicrobial activities of 9 bacteriocin-like substance (BLS)­producing strains were evaluated after growing them on defatted soybean meal medium (DSMM). Bacillus subtilis was selected among those, because it showed the biggest inhibition zone against 6 problem bacteria in food. The antimicrobial edible film, containing $0.32\%$ of BLS, was produced from the fermented soybean meal with B. subtilis at the optimum condition of pH 7.0-7.5 and $33^{\circ}C$ for 33 h. The antimicrobial activity of the film was over $50\%$ of the maximum activity after film production with heat treatment at $90^{\circ}C$ and pH adjustment to 9. When the soy protein film with BLS was applied on the agar media containing E. coli, the growth inhibition was much higher than the ordinary soy protein film. These results indicate that the soy protein film with BLS from B. subtilis can be used as a new packaging material to extend the shelf-life of foods.

• Molecules and Cells
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• v.38 no.3
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• pp.273-278
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• 2015

The induction of angiogenesis is a crucial step in tumor progression, and therefore, efficient inhibition of angiogenesis is considered a powerful strategy for the treatment of cancer. In the present study, we report that the lipophilic antimicrobial peptides from EML-CAP3, a new endophytic bacterial strain isolated from red pepper leaf (Capsicum annuum L.), exhibit potent antiangiogenic activity both in vitro and in vivo. The newly obtained antimicrobial peptides effectively inhibited the proliferation of human umbilical vein endothelial cells at subtoxic doses. Furthermore, the peptides suppressed the in vitro characteristics of angiogenesis such as endothelial cell invasion and tube formation stimulated by vascular endothelial growth factor, as well as neovascularization of the chorioallantoic membrane of growing chick embryos in vivo without showing cytotoxicity. Notably, the angiostatic peptides blocked tumor cell-induced angiogenesis by suppressing the expression levels of hypoxia-inducible $factor-1{\alpha}$ and its target gene, vascular endothelial growth factor (VEGF). To our knowledge, our findings demonstrate for the first time that the antimicrobial peptides from EML-CAP3 possess antiangiogenic potential and may thus be used for the treatment of hypervascularized tumors.