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Jin-Gyu Park,Hiroki Saeki,Atsushi Nakamura,Koth-Bong-Woo-Ri Kim,Ju-Woon Lee,Myung-Woo Byun,Seong-Mi Kim,Sung-Mee Lim,Dong-Hyun Ahn 한국식품과학회 2007 Food Science and Biotechnology Vol.16 No.6
Saeujeot (salted and fermented shrimp) and kimchi are traditional Korean fermented foods. Even though shrimp have often induced severe allergic reactions in sensitized individuals, few studies have investigated the allergenicity of shrimp. The aim of this study was to observe the changes of pH and allergenicity of raw shrimp (Acetes japonicus) and saeujeot in cabbage kimchi during fermentation using competitive indirect enzyme-linked immunosorbent assay (Ci-ELISA). Fermentation was carried out at different temperatures (25, 15, and 5℃). The pH of cabbage kimchi added with raw shrimp or saeujeot slowly decreased at lower temperature (5℃) at the end stage of the fermentation process. The binding ability of serum obtained from patients allergic to raw shrimp against shrimp tropomyosin and saeujeot in kimchi rapidly decreased during longer fermentation periods and higher temperature (25℃). In conclusion, the allergenicity of both raw shrimp and saeujeot in kimchi decreased during fermentation but the decrease in allergenicity of saeujeot was greater than observed for raw shrimp.
Nakamura, Soichiro,Ogawa, Masahiro,Saeki, Hiroki,Saito, Masayoshi,Miyasaka, Satoko,Hata, Junya,Adachi, Naoko,Hwang, Jae-Kwan The Korean Society of Food Science and Nutrition 2000 Preventive Nutrition and Food Science Vol.5 No.4
Protein conjugation of curdlan belonging to $\beta$-1, 3-glucan was carried out to improve it surface functionalities. The glucan was mixed with phosvitin, {TEX}$$\alpha$_{s}${/TEX}-casein, lysozyme or ovalbumin, respectively. The mixture was freeze-dried, and he resulting powder was incubated at 6$0^{\circ}C$ and 79% relative humidity for 12 days in order to generate a controlled Maillard reaction between curdlan and proteins. conjugation with unfolding proteins, i.e., phosvitin and {TEX}$$\alpha$_{s}${/TEX}-casein, drastically increased the solubility of the glucan, whereas lysozyme and ovalbmin did not. The solubility in water of curdlan was 3.44% for the phosvitin conjugate and 1.09% for the {TEX}$$\alpha$_{s}${/TEX}-casein conjugate. SDS-slab polyacrylamide gel electrophoresis showed that curdlan was solubilized due to covalent binding with phosvitin. Emulsifying properties of curdlan were substantially improved by the conjugation with phosvitin and {TEX}$$\alpha$_{s}${/TEX}-casein. Emulsion stability of the curdlan-phosvitin conjugate was about 2.9 times greater than that of the curdlan-phosvitin mixture.
Soichiro Nakamura,Masahiro Ogawa,Hiroki Saeki,Masayoshi Saito,Satoko Miyasaka,Junya Hata,Naoko Adachi,Jae-Kwan Hwang 한국식품영양과학회 2000 Preventive Nutrition and Food Science Vol.5 No.4
Protein conjugation of curdlan belonging to β-1,3-glucan was carried out to improve its surface functionalities. The glucan was mixed with phosvitin, α_s-casein, lysozyme or ovalbumin, respectively. The mixture was freeze-dried, and the resulting powder was incubated at 60℃ and 79% relative humidity for 12 days in order to generate a controlled Maillard reaction between curdlan and proteins. Conjugation with unfolding proteins, i.e., phosvitin and α_s-casein, drastically increased the solubility of the glucan, whereas lysozyme and ovalbumin did not. The solubility in water of curdlan was 3.44% for the phosvitin conjugate and 1.09% for the α_s-casein conjugate. SDS-slab polyacrylamide gel electrophoresis showed that curdlan was solubilized due to covalent binding with phosvitin. Emulsifying properties of curdlan were substantially improved by the conjugation with phosvitin and α_s-casein. Emulsion stability of the curdlan-phosvitin conjugate was about 2.9 times greater than that of the curdlan-phosvitin mixture.
Soichiro Nakamura,Masayoshi Saito,Tetsuhisa Goto,Hiroki Saeki,Masahiro Ogawa,Masayuki Gotoh,Yasuhide Gohya,Jae-Kwan Hwang 한국식품영양과학회 2000 Preventive Nutrition and Food Science Vol.5 No.2
Hen egg-white lysozyme was conjugated with 7~9 mers xyloglucan hydrolysates (MW=1,400) at 60℃ and 79% relative humidity for 3 days. SDS-PAGE showed that the conjugation between lysozyme and the oligosaccharide began from 1-day incubation, and three molecules of carbohydrate chains were attached to a protein molecule after 3-day incubation. The enzymatic activity of lysozyme was totally conserved in the neoglycoprotein, when measured by using glycol chitin as substrate. Besides, the emulsifying properties of lysozyme were vastly improved by the conjugation with the oligosaccharide, in which emulsifying activity of the neoglycoprotein was five times higher than that of native one.
Soichiro Nakamura,Kazumi Dokai,Megumi Matsuura,Junya Hata,Hiroki Saeki 한국식품영양과학회 2002 Preventive Nutrition and Food Science Vol.7 No.2
Hen egg-white lysozyme, ovalbumin, egg-yolk phosvitin, acid-precipitated soy protein, αs1 milk casein were covalently linked with galactomannan through a controlled dry-heating at 60℃ under 79% relative humidity without any chemical reagent. Neoglycosylation by the covalent binding of polysaccharide chains brought a significant improvement into the surface functionalities of food proteins. Excellent emulsifying properties, foaming properties were observed in all protein-galactomannan conjugates. Bacterial mutagenesis tests, animal dose test were done to evaluate the food safety of the protein-galactomannan conjugates. The neoglycoproteins were negative for Ames test using Salmonella typhimurium TA100 (hisG46), TA98 (hisD3052) strains,, rec-assay using Bacillus subtilis H17 (rec^-), M45 (rec^+) strains. All substances were also nontoxic for oral administration to rats. LD_(50)’s of these substances were all more than 7.5 g/kg body-weight of rat. No effect was also observed in the weight increases, the concentrations of total cholesterol, triglyceride, phospholipids in blood serum of the administrated rats with 7.5 g/kg conjugates. Thus, Maillard-type proteinpolysaccharide conjugates prepared by covalent attachment of galactomannan to food proteins were proposed to be useful as a safe functional biopolymer in this study.
Changes in the Allergenicity of Saeujeot by Fermentation
Seong Mi Kim,Jin Gyu Park,Koth-Bong-Woo-Ri Kim,Hiroki Saeki,Atsushi Nakamura,Ju Woon Lee,Myung Woo Byun,Dong Hyun Ahn 한국식품과학회 2008 Food Science and Biotechnology Vol.17 No.5
The aim of this study was to observe the changes in allergenicity of saeujeot (salted and fermented shrimp) using a competitive indirect enzyme-linked immunosorbent assay (Ci-ELISA). The fermentation conditions tested for saeujeot consisted of various temperatures (25, 15, and 5℃) and salt concentrations (25, 15, and 10%). When saeujeot was fermented at a low salt concentration and high temperature, the binding ability of mAb and shrimp-allergic patient serum to allergen was significantly decreased. In particular, the binding ability of mAb to allergen in saeujeot fermented with 10% salt at 25℃ for 5 days decreased to 5%. Also, the binding ability of shrimp-allergic patient serum to allergen in saeujeot fermented for 5 days with 10% salt at 25℃ was 8%. In conclusion, the binding of mAb and shrimp-allergic patient serum to tropomyosin in saeujeot decreased with longer fermentation periods, lower salt concentrations (10%), and higher temperatures (25℃).
Nakamura, Soichiro,Dokai, Kazumi,Matsuura, Megumi,Hata, Junya,Saeki, Hiroki The Korean Society of Food Science and Nutrition 2002 Preventive Nutrition and Food Science Vol.7 No.2
Hen egg-white lysozyme, ovalbumin, egg-yolk phosvitin, acid-precipitated soy protein and $\alpha$$_{sl}$ milk casein were covalently linked with galactomannan through a controlled dry-heating at 6$0^{\circ}C$ under 79% relative humidity without any chemical reagent. Neoglycosylation by the covalent binding of polysaccharide chains brought a significant improvement into the surface functionalities of food proteins. Excellent emulsifying properties and foaming properties were observed in all protein-galactomannan conjugates. Bacterial mutagenesis tests and animal dose test were done to evaluate the food safety of the protein-galactomannan conjugates. The neo-glycoproteins were negative for Ames test using Salmonella typhimurium TA100 (hisG46) and TA98 (hisD3052) strains, and rec-assay using Bacillus subtilis Hl7 (rec) and M45 (re $c^{+}$) strains. All substances were also nontoxic for oral administration to rats. L $D_{50}$ 's of these substances were all more than 7.5 g/kg body-weight of rat. No effect was also observed in the weight increases and the concentrations of total cholesterol, triglyceride and phospholipids in blood serum of the administrated rats with 7.5 g/kg conjugates. Thus, Maillard-type protein-polysaccharide conjugates prepared by covalent attachment of galactomannan to food proteins were proposed to be useful as a safe functional biopolymer in this study.y.