• Journal of Food Hygiene and Safety
• /
• v.10 no.4
• /
• pp.199-204
• /
• 1995

The antifungal effects of polyposphates on the growth and T-2 toxin production of Fusarium sporotrichioides M-1-1 were investigated. The growth of the strain was significantly inhibited in the potatoes dextrose agar medium treated with 1.5% polyphosphates or more. When we checked T-2 toxin by the indirect competitive ELISA, the strain produced 11.25 ug/ml and 10.90 ug/ml levels of T-2 toxin rice and corn containing 50% moisture contents, respectively. However, T-2 toxin was little detected in rice medium and corn medium with 1.5% polyphosphates addition for short(14 days) and prolonged incubation time(45 days). We also observed the destruction of cell wall and outflow of cell ingredients with 1% polyphosphates treatment to the strain. Therefore, moisture and polyphosphates greatly effected on the growth and T-2 toxin production of the strain.

• Korean Journal of Food Science and Technology
• /
• v.32 no.5
• /
• pp.991-996
• /
• 2000

Enzyme-linked immunosorbent assay was developed for the analysis of soy protein in foods. Competitive indirect ELISA (ciELISA) was established by using specific antibodies against the heat-stable acidic subunits (AS) of glycinin. Soy proteins in each sample used in this study were solublized in the presence of urea and DTT and boiled at $100^{\circ}C$ for 1hr and then were renatured with a cystine-containing solution. After these treatments, each isolated soy protein (ISP) heated at 60, 70, 80, $90^{\circ}C$ for 10 minutes showed almost the same curve as unheated one in the ciELISA. The detection limit of ISP was 0.3 ${\mu}g/mL$. Anti-AS antibodies have very low reactivities less than 0.1% toward non-meat proteins such as skim milk and casein and did not show any reactivities toward egg white powder and ovalbumin. When laboratory-made sausages containing ISP of $0.5{\sim}3%$ were assayed by ciELISA, the mean recovery was about 83% (C.V., 19%). In addition, the average content of soy protein in commercial sausages was 1.27%.

• Korean Journal of Food Science and Technology
• /
• v.36 no.1
• /
• pp.147-151
• /
• 2004

Antigenicities of ovomucoid (OM) and ovalbumin (OA) in chicken egg white (EW) before and after NaOH, heat, and pretense treatments were examined by competitive indirect enzyme-linked immunosorbent assay (ciELISA), using rabbit anti-OM and-OA antibodies, Enzymatic hydrolysis of EW did not effectively reduce antigenicity of OM, whereas that of OA was decreased to 1/5,000-1/100,000 by treatment of plant-derived or microbial pretenses. Heat treatment below $100^{\circ}C$ for 30min did not decrease antigenicity of OM, whereas that of OA in heated EW increased maximally to 100 times, Antigenicity of OM in EW effectively decreased by NaOH treatment, disappearing at over 1% NaOH, whereas that of OA increased. Additional heat treatment of NaOH-treated EW at $70^{\circ}C$ for 15min slightly reduced antigenicities of OM and OA.

• Korean Journal of Food Science and Technology
• /
• v.32 no.3
• /
• pp.720-725
• /
• 2000

To reduce the antigenicity of egg white (EW), EW was treated with several proteolytic enzymes, trifluoromethanesulfonic acid (TFMS), heat, and NaOH. Competitive indirect enzyme-linked immunosorbent assay (ciELISA), using rabbit anti-EW antibody, was performed to examine the antigenicity of the treated EW's. Enzymatic hydrolysis gave no good effect on the reduction of the antigenicity of EW. Neither did the pretreatment with ${\gamma}-irradiation$ before the hydrolysis reduce the antigenicity. TFMS treatment removed the antigenicity of EW. The antigenicity of EW heated at $120^{\circ}C$ for 30 min or treated with NaOH at 0.3% (w/v) and more, decreased to less than 1/10,000 as compared with that of native EW. The combinatory treatment with NaOH, followed by heat at $70^{\circ}C$ for 15 min had a synergic effect on the reduction of the antigenicity of EW.

• Korean Journal of Food Science and Technology
• /
• v.30 no.6
• /
• pp.1409-1414
• /
• 1998

To develop zearalenone-specific monoclonal antibodies, hybridoma cells were produced by fusion of myeloma cells $(P3{\times}63Ag\;V653)$ and spleen cells from BALB/c female mice immunized with zearalenone-oxime coupled to bovine serum albumin (BSA). After screening of antibody titer of them with a sandwich type enzyme-linked immunosorbent assay (ELISA), 5 hybridomas which could produced monoclonal antibodies with a high affinity for zearalenone were selected. The monoclonal antibody produced by Z-2-M26 hybridoma exhibited the high sensitivity to zearalenone and a little cross-reactivity to ${\alpha}-zearalenol$ (11%), but did not react with ${\beta}-zearalenol,\;{\alpha}-zearalenol,\;{\beta}-zearalenol$ and DON. In conclusion, the developed monoclonal antibody appeared to be a very promising immunoreagent for the future development of a specific and sensitive quantitative ELISA for zearalenone.

• Korean Journal of Food Science and Technology
• /
• v.30 no.4
• /
• pp.862-870
• /
• 1998

This study shows the application of Ci-ELISA method for monitoring the denaturation of myosin by the frozen treatment in order to differentiate thawed beef from chilled. Hanwoo M.Semitendinosus (n=25) was treated under the two different frozen process as follows; simple frozen treatment (Exp-1) at 4 different temperatures, -10, -20, -50 and $-80^{\circ}C$, respectively, and repeated thawing-refreezing treatment (Exp-2) stored at 4 different temperatures, -10, -20, -50 and $-80^{\circ}C$, respectively. Antibodies (Abs) were produced from rabbits immunized with myosin whole molecule (MWM) isolated from beef round, heavy meromyosin S-1 (S-1) and light meromyosin (LMM) prepared by digestion of MWM. Each immunoglobulin G (IgG) was separated from antiserum. At 6 month storage, IA of anti-MWM IgG for myosin was decreased to 32.67, 32. 23, 51.52 and 34.27% in Exp-1 and to 14.82, 15.61, 25.3 and 23.7% in Exp-2 at -10, -20, -50 and $-80^{\circ}C$, respectively (P<0.05). In Exp-1, the reactivities of anti-LMM IgG were decreased to 25.12, 21.42, 49.05 and 28.96%, and those of Exp-2 were to 11.88, 9.56, 20.63 and 12.64% at -10, -20, -50 and $-80^{\circ}C$, respectively, at 6 times thawing (P<0.05). Conclusively, myosin was denaturated by freezing treatment and LMM or myosin rod part might have suffered from more extreme demage than HMM S-1, and samples at $-50^{\circ}C$ were slightly injured less than others by freezing treatment.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.33 no.7
• /
• pp.1169-1174
• /
• 2004

This study was carried out to assess the effects of electron beam (EB) radiation on the conformational changes of ovalbumin (OVA), based on the early works using gamma irradiation. The applied doses of OVA used were 3,5,7, and 10 kGy, respectively. The conformational alterations were measured with SDS-PAGE, GPC-HPLC, and competitive indirect enzyme-linked immunosorbent assay (Ci-ELISA) using monoclonal anti-OVA IgG antibody. Irradiation caused a degradation and/or an aggregation of OVA molecule. Immunochemical structures of irradiated OVA were altered by irradiation. Effects of gamma and electron beam radiation were similar at the same absorbed doses. These results may be used for inhibition of food allergy and development of immunogen with EB radiation.

• BMB Reports
• /
• v.31 no.1
• /
• pp.58-63
• /
• 1998

In this study, a mouse monoclonal antibody (mAb) against gp41(584-618), the immunodominant epitope protein, was generated. For this purpose, BALB/c mice were immunized with double branched multiple antigenic peptides derived from the HIV-1 gp41(584-618) sequence, and antibody-secreting hybridoma were produced by fusion of mice splenocytes with SP2/0 myeloma cells. One clone producing an antigen specific mAb, termed KI-41(isotype IgG1) was identified, whose specific reactivity against gp41(584-618) could be confirmed by ELISA and Western blot analysis. Epitope mapping revealed the recognition site of the mAb KI-41 to be located around the sequence RILAVERYLKDQQLLG, which comprises the N-terminal region within the immunized gp41(584-618) peptied. Since this mAb recognizes this specific epitope within the HIV-1 gp41 without any cross-reactivity to other immunodominant regions in the HIV-2 gp35, KI-41 will provide some alternative possibilities in further applications such as the development of indirect or competitive ELISA for specific antibody detection in HIV-1 infection or for other basic researches regarding the role and function of HIV-1 gp41.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.30 no.3
• /
• pp.505-509
• /
• 2001

This study was carried out to evaluate the application of food irradiation technology as a method for reducing milk allergies. Bovine $\alpha$-casein, $\beta$-casein, $textsc{k}$-casein, $\alpha$-lactalbumin(ALA), $\beta$-lactoglobulin (BLG) and serum albumin (BSA) were used as model allergens of milk proteins and the proten solution (2.0 mg/mL) with 0.01 M phosphate buffered saline (pH 7.4) was irradiated at 3, 5 and 10 kGy. Using milk-hypersensitive patients IgE (MHP-IgE), the changes of binding ability to irradiated proteins were observed by competitive indirect enzyme-linked immunosorbent assay (Ci-ELISA). Affinity of MHP-IgE to milk proteins was higher in ALA and BLG than that of other proteins. Standard curve to each non-irradiated protein could be made with MHP-IgE for quantifying milk allergens. Binding abilities of MHP-IgE to the irradiated proteins, however, decreased with different slopes of the standard curves. Sensitivity of gamma irradiation was higher in ALA and BLG than of other proteins. These results indicated that irradiation technology can be used to reduce the milk hypersensitivity.

• Food Science and Biotechnology
• /
• v.17 no.5
• /
• pp.919-924
• /
• 2008

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 $5^{\circ}C$) 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 $25^{\circ}C$ 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 $25^{\circ}C$ 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 ($25^{\circ}C$).