• Journal of the Korean Society of Food Culture
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• v.28 no.6
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• pp.664-673
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• 2013

This study was conducted to investigate the physicochemical properties of mung bean starch and the quality characteristics of mung bean starch gels supplemented with gelatin and isolated soy protein (0, 2, 5%) during storage at $5^{\circ}C$ for 0, 24, 48, and 72 hours. The swelling power of mung bean starch supplemented with gelatin did not significantly change, whereas those supplemented with isolated soy protein (ISP) significantly increased. The solubility of mung bean starch supplemented with gelatin and ISP, however, significantly increased with increasing concentration. In addition, the soluble amylose and soluble carbohydrate of mung bean starch supplemented with gelatin and ISP significantly decreased with increasing concentration. In terms of pasting properties measured by the Rapid Visco Analyzer (RVA), the pasting temperature of mung bean starch supplemented with gelatin and ISP was not significantly different, whereas peak viscosity, minimum viscosity, final viscosity, breakdown, and consistency decreased. DSC thermograms showed that the onset temperature of mung bean starch supplemented with gelatin and ISP did not significantly change, whereas the enthalpy increased with the addition of 5% ISP. The lightness (L) and redness (a) of mung bean starch gels supplemented with gelatin, ISP, and without additives increased during cold storage, whereas the yellowness (b) decreased. The addition of gelatin and ISP suppressed changes in L, a and b of mung bean starch gel during cold storage. Synereses of mung bean starch gel supplemented with gelatin and ISP was lower than that without additives, with the addition of gelatin suppressing synereses more than ISP. The addition of gelatin and ISP also suppressed increases in hardness, chewiness, and gumminess of mung bean starch gels during cold storage. In the sensory evaluation, the addition of gelatin and ISP suppressed increases in hardness and brittleness of mung bean starch gels during cold storage. The addition of 2%, 5% gelatin and 2% ISP also suppressed a decrease in the overall acceptability of mung bean starch gels during 24-48 hr cold storage. Thus, the addition of 2-5% gelatin and 2% ISP to mung bean starch is appropriate for suppressing the quality deterioration of 24-48 hr cold-stored mung bean starch gels.

• Polymer(Korea)
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• v.29 no.5
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• pp.457-462
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• 2005

Polyurethane foams (PUFs) were prepared from polymeric 4,4'-diphenylmethane diisocyanate (PMDI), mixed polyol with OH value of 480, silicone surfactant, three catalysts, and hydrofluorocarbon(HFC) as blowing agent. Balance (PC-8), gelling (33LV), and trimerization (TMR-2) catalysts were used. The effect of the catalysts on the physical properties of PUF with increase of isocyanate (NCO) index and aging time was investigated. The cell size of the PUF with PC-8 and 33LV slightly increased with an increase in NCO index from 100 to 170 but compressive strength did not change significantly. In case of trimerization catalyst, the compressive strength of PUF increased from 8.75 to 1$10.5 kg_f/cm^2$ and the cell size decreased with an increase in NCO index. The compressive strength of the PUF with 33LV increased from 9.21 to $10.15 kg_f/cm^2$ with an increase in aging time. However, there was no detectable change in the compressive strength of PUF with TMR-2. A possible interpretation of the results includes an additional cross-link reaction of non-reacted MDI and FTIR spectrum illustrated the change of NCO peak.

• Korean Journal of Food Science and Technology
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• v.46 no.5
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• pp.593-600
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• 2014

Normal rice starch (NRS) possesses high gelling and retrogradation tendencies, with poor freeze-thaw stability. This study investigated the effects of partial replacement of waxy rice starch (WRS) with gums on the pasting and viscoelastic properties as well as the freeze-thaw stability of the WRS paste. Xanthan gum (XAT), locust bean gum (LBG), and their mixtures were individually mixed with WRS at a ratio of 1:19 (w/w). WRS-gum mixtures were pasted using a rapid visco-analyzer at 5% total solid content, and analyzed with respect to the pasting and viscoelastic characteristics, and freeze-thaw stability. Pasting properties of WRS were retarded in pasting temperature and enhanced in pasting viscosity (although peak viscosity was varied) by partial replacement with gum and gum mixtures. Storage moduli of WRS-XAT:LBG pastes became similar to those of NRS paste with increasing angular frequency from 1 to 10 rad/s. Finally, WRS-XAT and WRS-XAT:LBG possessed more enhanced freeze-thaw stability than NRS.

• Culinary science and hospitality research
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• v.15 no.4
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• pp.99-114
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• 2009

This study examined the optimal cooking condition for surimi-like material (SLM) derived from porcine semimembranosus (SM) muscle and the effects of the various cooking temperatures and the cooking time on the gel properties. The most noticeable change that occurred during the preparation of the SLM from the SM was the reduction in the fat content (about 1%) during the washing procedures. The hardness and gel strength value were increased significantly as the cooking temperature was increased by $75^{\circ}C$ for 20 min (p<0.05). The SLMG cooked above $75^{\circ}C$ had a significantly higher WHC than the SLMG cooked below $75^{\circ}C$ (p<0.05). The gelling property of SLMG was effected for different conditions of cooking time and temperatures by the result of SDS-PAGE. After 20 min cooking, some enzyme bands including phosphorylase disappeared. The loss of these bands (about 46 kDa and 60 kDa) was observed after 20 min of cooking time. The photographs of microscopy showed that the filaments of myofibrils did not disappear after a cooking time of 15 min, and that the gaps between the fibers or filament were close. A significant change in the fibers and filaments occurred from 30 min to 35 min of cooking time, and the gradual coagulation of the structure of the SLM was observed with cooking time increased. These results suggest that a desirable surimi gel could be obtained from pork by cooking at $75^{\circ}C$ for 25 min.

• Applied Biological Chemistry
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• v.36 no.6
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• pp.440-448
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• 1993

To utilize effectively fish skin wasted from fish processing, a dover sole skin gelatin was prepared by alkaline extraction method and the physico-chemical properties were examined. Conditions for the suitable pretreatment, extraction and decolorization for gelatin preparation from dover sole skin are as follows: the skin is limed with 1.0% calcium hydroxide solution at $5^{\circ}C$ for 4 days, washed thoroughly for 2 days with tap water, extracted with 5 volumes of water $(pH\;5.0{\sim}7.0)$ to dehydrated skin for 3 hours at $50^{\circ}C$, and then bleached with 3% activated carbon. Though dover sole skin gelatin was prepared under above conditions, physico-chemical property values such the melting point and gelling point of that were lower than those of yellowfin sole skin gelatin as well as the commercial pork skin gelatin. Therefore, the purified dover sole skin gelatin requires a suitable modification operation for better quality gelatin manufacture.

• Applied Biological Chemistry
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• v.36 no.4
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• pp.290-295
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• 1993

In order to utilize effectively fish skin from fish processing, characteristics of the yellowfin sole and dover sole skins were investigated. In the yellowfin sole, the crude protein content and yield of fish skin used for the preparation of gelatin were 22.3% and 11.3%, respectively and in the dover sole, 17.2% and 8.9%, respectively. In the yellowfin sole skin, the soluble and insoluble collagen occupied 66.1% and 33.9%, respectively and in the dover sole skin, 78.8% and 21.1%, respectively. No difference in the amino acid composition between soluble and insoluble collagen was detected. The sum of proline and hydroxyproline content in the collagen extracted from fish skin was lower than that of those from pork skin or bone. The molecular weight of the two major subunits from the soluble collagen in the yellowfin sole skin were found to be 143 KDa and 202 KDa. Those in the dover sole skin were 142 KDa and 207 KDa. The physico-chemical properties such as the melting point and gelling point of yellowfin sole skin gelatin were superior to those of dover sole skin gelatin.

• Korean Journal of Food Science and Technology
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• v.25 no.6
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• pp.716-723
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• 1993

To utilize effectively fish skin wasted from fish processing, a yellowfin sole skin gelatin was prepared by alkaline extraction method and the physico-chemical properties were examined. Conditions for the suitable extraction and decolorization for gelatin preparation from yellowfin sole skin are as follows: the skin is limed with 1.5% calcium hydroxide solution at $5^{\circ}C$ for 5 days, washed throughly with tap water, extracted with 6 volumes of water ($pH5.0{\sim}7.0$) to dehydrated skin for 3 hours at $50^{\circ}C$, and then bleached with 3% activated carbon. Though yellowfin sole skin gelatin was prepared under above condition, the physico-chemical property values such the melting point and gelling point of that were lower than those of pork skin gelatin. Therefore, the purified yellowfin sole skin gelatin requires a suitable modification operation for more a good quality gelatin manufacture.

• Applied Biological Chemistry
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• v.39 no.2
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• pp.134-139
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• 1996

In order to effectively utilize marine animal skin wastes in marine processing manufacture, conger eel skin, file fish skin and arrow squid skin as raw material of edible gelatin were screened. Conger eel skin was the highest in the collagen content, followed by Ole fish skin and arrow squid skin, in the order named. In the fish skins, the soluble and insoluble collagens occupied $67.4%{\sim}72.3%\;and\;27.7{\sim}32.6%$, respectively, and in the arrow squid skin, 30.4ft and 69.6ft, respectively. No difference in the amino acid composition between soluble and insoluble collagens was detected. Collagen from the marine animal skin catched in coasted and offshore water in Korea consisted ${\alpha}$ chain and ${\beta}$ chain, and ${\alpha}$ chain were hetero type. The sum of proline and hydroxyproline contents in conger eel skin collagen was higher than that in the other skin collagens, while was lower than that pork skin collagen. Conger eel skin collagen exhibited a higher denaturation temperature in solution and a higher degree of proline hydroxylation, compared with skin collagen of the respective species. The physical properties such as gel strength, melting point and gelling point of conger eel skin gelatin were superior to those of file fish skin and arrow squid skin gelatins.

• Applied Biological Chemistry
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• v.39 no.4
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• pp.274-281
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• 1996

To prepare edible skin gelatin of conger eel such as material fur quality improvement of surimi gel, the defatted skin was limed with 1% calcium hydroxide at $5^{\circ}C$ for 2 days, washed thoroughly with tap water, extracted with 8 volumes of distilled water to dehydrated skin for 2 hours at $50^{\circ}C$. The gelatin extract was centrifuged, filtered and then passed through anion(Amberlite 200C) and cation (Amberlite IR 900) resins. The purified gelatin solution was evaporated and dried by hot-air blast$(40^{\circ}C)$. The gelatin prepared by above condition had the highest quality as revealed by physical property values i.e. 240.5 g in gel strength, $28.0^{\circ}C$ in melting point and $28.0^{\circ}C$ in gelling point. Funtional property values were 56.8% in solubility, 1.8 ml/g in oil binding capacity, 55.0% in emulsifying capacity and 48.5% in emulsifying stability. jelly strength and senso교 evaluation of surimi gel from fish with red muscle were not improved by addition of emulsifying curd from conger eel skin gelatin as emulsifier. Therefore, the conger eel skin gelatin requires a suitable modification of functional group and improvement of processing operation to utilize as a material for quality Improvement of surimi gel.

• Korean Chemical Engineering Research
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• v.49 no.4
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• pp.475-479
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• 2011

Chitosan is a natural polymer that has many physicochemical(polycationic, reactive OH and $NH_2$ groups) and biological(bioactive, biocompatible, and biodegradable) properties. In this study, chitosan nanoparticles were prepared using poly-${\gamma}$-glutamic acid(${\gamma}$-PGA) as gelling agent. Nanoparticles were formed by ionic interaction between carboxylic groups in ${\gamma}$-PGA and amino groups in chitosan. Chitosan(0.1~1 g) was dissolved in 100 ml of acetic acid (1% v/v) at room temperature and stirred overnight to ensure a complete solubility. An amount of 0.1 g of ${\gamma}$-PGA was dissolved in 90 ml of distilled water at room temperature. Chitosan solution was dropped through needle into beaker containing ${\gamma}$-PGA solution under gentle stirring at room temperature. The average particle sizes were in the range of 80~300 nm. The prepared chitosan/${\gamma}$-PGA nanoparticles were used to examine their removal of several heavy metal ions($Cd^{2+}$, $Pb^{2+}$, $Zn^{2+}$, $Cu^{2+}$, and $Ni^{2+}$) as adsorbents in aqueous solution. The heavy metal removal capacity of the nanoparticles was in the order of $Cu^{2+}$ > $Pb^{2+}$ > $Cd^{2+}$ > $Ni^{2+}$ > $Zn^{2+}$.