• Korean Journal of Food Science and Technology
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• v.40 no.6
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• pp.611-620
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• 2008

The principal objective of this study was to assess the effects of phosphatidylcholine (PC) and phosphatidylethanolamine (PE) extracted from egg yolk on the oxidation of tocopherol-stripped canola oil and its browning, as well as their content changes during 12 hr of heating at $180^{\circ}C$. PC and/ or PE contents in the oil were measured at 200, 500, 1,000, or 2,000 ppm. PL contents in the oil and oil browning were determined by high performance liquid chromatography (HPLC) and spectrophotometry, respectively. The oil oxidation was evaluated by the combination of fatty acid composition, conjugated dienoic acid content, and p-anisidine value. PC was degraded at a slower rate than PE during heating and the co-presence of PE reduced its rate of degradation. PE increased oil browning more profoundly than PC did. PC significantly reduced oil oxidation during heating; however, we noted a possible antagonism between PE and PC in reducing the oil oxidation. Egg yolk PC was a better antioxidant in oil oxidation during heating.

• Journal of Integrative Natural Science
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• v.3 no.2
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• pp.72-77
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• 2010

Alginate lyases, also known as alginases or alginate depolymerases, catalyze the degradation of alginate by a ${\beta}$-elimination mechanism that has yet to be fully elucidated. Alginate is a copolymer of ${\alpha}$-L-guluronate (G) and its C5 epimer ${\beta}$-D-mannuronate (M), arranged as homopolymeric G blocks, M blocks, alternating GM or random heteropolymeric G/M stretches. Almost all alginate lyases depolymerize alginate in an endolytical fashion via a ${\beta}$-elimination reaction. The alginate lyase Atu3025 from Agrobacterium tumefaciens strain C58, consisting of 776 amino-acid residues, is a novel exotype alginate lyase classified into polysaccharide lyase family 15. Till now there is no crystal structure available for this class of proteins. Since there is no template with high sequence identity, three-dimensional coordinates for exotype alginate lyase (PL 15 family) were determined using modeling methods (Comparitive modeling and Fold recognition). The structures were modeled using the X-ray coordinates from Heparinase protein family (PDB code: 3E7J). This enzyme (Atu3025) displays enzymatic activity for both poly-M and poly-G alginate. Since poly-M is widespread; docking of a tri-mannuronate against the modeled structure was performed. We identified some of those residues which are crucial for lyase activity. The results from this study should guide future mutagenesis studies and also provides a starting point for further proceedings.

• Journal of the Korean Applied Science and Technology
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• v.34 no.1
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• pp.50-57
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• 2017

Zinc oxide is, one of metal oxide semiconductor, harmless to human and environment-friendly. It has excellent chemical and thermal stability properties. Wurtzite-zinc oxide is a large band gap energy of 3.37 eV and high exciton binding energy of 60 meV. It can be applied to various fields, such as solar cells, degradation of the dye waste, the gas sensor. The photocatalytic activity of zinc oxide is varied according to the particle shape and change of crystallinity. Therefore, It is very important to specify the additives and the experimental variables. In this study, the zinc oxide were synthesized by using a microwave assisted hydrothermal synthesis. The precursor was used as the zinc nitrate, the pH value was controlled as 11 by NaOH. Surfactants are the ethanolamine, cetyltrimethylammonium bromide, sodium dodecyl sulfate, sorbitan monooleate was added by changing the concentration. The composite particles had the shape of a star-like, curcular cone, seed shape, flake-sphere. Physical and chemical properties of the obtained zinc oxide was characterized using x-ray diffractometer, field emission scanning electron microscopy, thermogravimetric analysis and optical properties was characterized using UV-visible spectroscopy, photoluminescence and raman spectroscopy.

• Journal of Life Science
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• v.27 no.11
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• pp.1276-1289
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• 2017

This study isolated and purified the antimicrobial peptide McSSP-31 from an acidified hemocyte extract of a Mytilus coruscus. The antimicrobial peptide was purified by using a $C_{18}$ reversed-phase high-performance liquid chromatography (HPLC). The peptide was determined to be 3330.549 Da by matrix assisted-laser desorption ionization time-of-flight mass spectrophotometer (MALDI-TOF/MS). The N-terminus of a 14 amino-acid sequence was identified as P-S-P-T-R-R-S-T-S-R-S-K-S-R by Edman degradation method. The acquired sequence showed a 93% similarity with the sperm-specific protein Phi-1, which is from M. californianus. The identified open-reading frame (ORF) of peptide was 306 bp encoding 101 amino acids, which was analyzed by rapid amplification of cDNA ends (RACE), cloning and sequencing analysis. We compared the full sequence with other known proteins that reveal the sperm-specific protein Phi-1 (93.5%) of M. californianus. Synthesized antimicrobial peptide (McSSP-31) showed antibacterial activity against gram-positive bacteria including B. subtilis, S. mutans, S. aureus and gram-negative bacteria including E. coli, K. pneumoniae, P. mirabilis, P. aeruginosa and fungi, C. albicans. Also, synthesized peptide showed strong antibacterial activity against antibiotic-resistant strains, including S. aureus. The cytotoxicity of the peptide was determined by using the HUVEC human cell line. The peptide did not exhibit any significant cytotoxic effects on the normal human cell line, and it had very low hemolytic activity with flounder hemoglobin. The results demonstrated that peptide purified from the hemocyte of a M. coruscus exhibits antibacterial activity against various bacteria and has the potential to be an alternative antibiotic agent.