• Korean Journal of Food Science and Technology
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• v.2 no.2
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• pp.30-33
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• 1970

This studies' objective methods of identifying fish species are based on the species-specific protein-separation patterns obtained on electrophoresis of watersoluble sarcoplasmic proteins of fish muscle. As the proteins must be in their native undenatured state, electrophoretic identification of fish species has, so far, been restricted to raw fish. An extention of the electrophoretic method to the identification of cooked fish is discribed. The protein fragments extractable in 10M urea from the denatured proteins of cooked muscle can also be separated by electrophoresis into species' characteristic patterns that could be used for species identification. The separation patterns obtained on polyacrylamide gel for the urea extracts of cooked Mugil cephalus, Gadus macrocephalus, Scomberomorus niphonius, Scomber japonicus, Pseudosciaena manchurica, Seriola quinqueradiata, Trichius lepturus, Duderleinia berycoides, Lophimus setigerus, Pampus argenteus are presented. In its present form the method does not apply to canned fish.

• Journal of Microbiology and Biotechnology
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• v.26 no.12
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• pp.2127-2137
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• 2016

A mangrove microbial community was analyzed at the gene and protein levels using metagenomic and proteomic methods with the green macroalgae Enteromorpha prolifera as the substrate. Total DNA was sequenced on the Illumina HiSeq 2000 PE-100 platform. Two-dimensional gel electrophoresis in combination with liquid chromatography tandem mass spectrometry was used for proteomic analysis. The metagenomic data revealed that the orders Pseudomonadales, Rhizobiales, and Sphingomonadales were the most prevalent in the mangrove microbial community. By monitoring changes at the functional level, proteomic analyses detected ATP synthase and transporter proteins, which were expressed mainly by members of the phyla Proteobacteria and Bacteroidetes. Members of the phylum Proteobacteria expressed a high number of sugar transporters and demonstrated specialized and efficient digestion of various glycans. A few glycoside hydrolases were detected in members of the phylum Firmicutes, which appeared to be the main cellulose-degrading bacteria. This is the first report of multiple "omics" analysis of E. prolifera degradation. These results support the fact that key enzymes of glycoside hydrolase family were expressed in large quantities, indicating the high metabolic activity of the community.

• Korean Journal of Food Science and Technology
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• v.23 no.6
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• pp.695-701
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• 1991

Spent layer breast meat and leg meat samples washed with 0.05 M sodium bicarbonate solution and 0.04 M phosphate buffer(pH 8.3) showed decreases in heat denaturation temperature indicating the destabilization of myofibrillar proteins. The destabilization was attributed to the solubilization of 95 Kdalton and 55 kdalton proteins from the myofibrils observed in gel-electrophoretograms. Transmission electron microscopy further indicated the breakage of Z-lines.

• Journal of the Korean Society of Food Science and Nutrition
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• v.27 no.3
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• pp.508-517
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• 1998

We investigated the effects of godulbaegi extracts on the physiochemical properties of biological membranes as membrane stability and fluidity employing the phospholipid liposomal membrances as a biomembrane-mimetic system. The addition of the godulbaegi extracts to the phospholipid exterted great effects stagbilized the barrier function of the liposomal membranes in proportion to the concentration of the additive and significantly increased the membranes fluidity. The values of the fluorescence polarization of 1,6-diphenyl 1,3,5-hexatriene (DPH) decreased gradually as the temperature increased, and decreased abruptly near the phase transition temperature (Tm) of the liposome from gel to liquid crystalline state as usual. These results suggest that the activities of the godulbaegi extracts to enhance the stability and fluidity of the liposomal membranes have implication in their biological activities.

• Food Science and Biotechnology
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• v.16 no.6
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• pp.902-909
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• 2007

Granular maize starch was treated with Thermus scotoductus 4-${\alpha}$-glucanotransferase (${\alpha}$-GTase), and its physicochemical properties were determined. The gelatinization and pasting temperatures of ${\alpha}$-GTase-modified starch were decreased by higher enzyme concentrations. ${\alpha}$-GTase treatment lowered the peak, setback, and [mal viscosity of the starch. At a higher level of enzyme treatment, the melting peak of the amylose-lipid complex was undetectable on the DSC thermogram. Also, ${\alpha}$-GTase-modified starch showed a slower retrogradation rate. The enzyme treatment changed the dynamic rheological properties of the starch, leading to decreases in its elastic (G') and viscous (G") moduli. ${\alpha}$-GTase-modified starch showed more liquid-like characteristics, whereas normal maize starch was more elastic and solid-like. Gel permeation chromatography of modified starch showed that amylose was degraded, and a low molecular-weight fraction with $M_w$ of $1.1{\times}10^5$ was produced. Branch chain-length (BCL) distribution of modified starch showed increases in BCL (DP>20), which could result from the glucans degraded from amylose molecules transferred to the branch chains of amylopectin by inter-/intra-molecular transglycosylation of ${\alpha}$-GTase. These new physicochemical functionalities of the modified starch produced by ${\alpha}$-GTase treatment are applicable to starch-based products in various industries.

• Journal of Applied Biological Chemistry
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• v.57 no.2
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• pp.183-188
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• 2014

In order to increase the nutritional quality of soybean meal (SBM) as an animal feed, Bacillus subtilis TP6, a previously isolated strain from an Indonesian traditional fermented soybean food, Tempeh, was used as a starter organism for solid-state fermentation. In the pre-treated SBM with water content of 60% (v/w), B. subtilis TP6 was grown to a maximum viable cell number of $3.5{\times}10^9CFU/g$. Compared to control, crude protein in Bacillus fermented SBM was increased by 16%, while raffinose, stachyose, and trypsin inhibitors were reduced by 31, 37, and 90%, respectively. The Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed that proteins in the fermented SBM were remarkably hydrolyzed into smaller molecular masses, resulting in a decrease in large sized proteins. Our data suggested that B. subtilis fermentation could increase the nutritive value of SBM through reduction of anti-nutritive factors and improvement of protein quality by hydrolysis of soy protein. In addition, B. subtilis TP6 produced a functional ingredient, poly-${\gamma}$-glutamic acid which has various health benefits.

• Food Science of Animal Resources
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• v.39 no.2
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• pp.209-221
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• 2019

In this study, the changes in microbial communities of lamb meat packaged in the air (plastic tray, PT) and in a vacuum pouch (VAC) were assessed by polymerase chain reaction-denaturing gradient gel electrophoresis (PCR-DGGE) during the storage at $4^{\circ}C$. For the PT lamb, the total viable count (TVC) was $10^7CFU/g$ on Day 5, and the dominated bacteria were Pseudomonas fragi, P. fluorescens, and Acinetobacter spp. For the VAC lamb, the TVC was $10^7CFU/g$ on Day 9, and the dominated bacteria were lactic acid bacteria, including Carnobacterium divergens, C. maltaromaticum, and Lactococcus piscium. One strain of Pseudomonas spp. also appeared in VAC lamb. The relative abundance of Enterobacteriaceae in VAC lamb was higher than that PT lamb, indicating a more important role of Enterobacteriaceae in spoilage for VAC lamb than that of PT lamb. The microbial compositions changed faster in the lamb stored in a PT than that stored in a VAC, and microbial community compositions of the late storage period were largely different from those of the early storage period for both the conditions. The findings of this study may guide improve the lamb hygiene and prolong the shelf life of the lamb.

• Nuclear Engineering and Technology
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• v.8 no.3
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• pp.145-150
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• 1976

Alkali-treated red algae, Gracilaria sp. was irradiated with various doses of cobalt-60 gamma-rays and the yeild and properties of agar extracted from the seaweed were examined and compared with the quality of commercial agar powder after irradiation. Extraction yield of agar from irradiated seaweed was proportionally increased as the radiation dose was raised up to 2 Mrad whereas it tended to decrease slightly thereafter. Gelation ability, gelation point, gel hardness and specific viscosity of the agar were increased up to 1 Mrad and decreased at higher dose levels while its melting point, total nitrogen, crude ash and total sulfur decreased up to 1 Mrad level and remained unchanged thereafter. Irradiation of commercial agar powder caused remarkable decreases in the gelation ability, specific viscosity and gel hardness and slight decreases in the gelation point and melting point. The pattern of alterations in the properties of agar samples differed whether the polysaccharide was irradiated in free state or bound state in seaweed.

• Korean Journal of Food Science and Technology
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• v.32 no.4
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• pp.822-827
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• 2000

Gamma irradiation was applied to reduce shrimp allergy. Shrimp heat-stable protein(HSP) and shrimp protein extract were gamma-irradiated at 1, 3, 5, 7 or 10 kGy in an aqueous state (1.0 mg/mL). The changes in allergenic and antigenic properties of protein extract and HSP resulted from gamma irradiation were monitored by ELISA with mouse mAb or human patients sera and immunoblotting. Conformational changes in irradiated HSP were measured by both GPC-HPLC and SDS-PAGE. The binding ability of shrimp allergic patients IgE to irradiated protein extract or irradiated heat-stable protein was dose-dependently reduced. When measured by gel permeation chromatography and sandwich ELISA, the amount of intact heat-stable protein in the irradiated solution was reduced by gamma irradiation depending upon the applied dose. SDS-PAGE showed that the main band disappeared and new bands appeared in a higher molecular weight zone. The results provide a new possibility to use irradiation process for reducing the allergenicity of shrimp.

• Journal of Microbiology and Biotechnology
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• v.22 no.9
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• pp.1253-1257
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• 2012

A gene (acas) designated as ${\alpha}$-amylase was cloned from Arthrobacter chlorophenolicus A6. The multiple amino acid sequence analysis and functional expression of acas revealed that this gene really encoded an amylosucrase (ASase) instead of ${\alpha}$-amylase. In fact, the recombinant enzyme exhibited typical ASase activity by showing both sucrose hydrolysis and glucosyltransferase activities. The purified enzyme has a molecular mass of 72 kDa and exhibits optimal hydrolysis activity at $45^{\circ}C$ and a pH of 8.0. The analysis of the oligomeric state of ACAS with gel permeation chromatography revealed that the ACAS existed as a monomer.