• Korean Journal of Food Science and Technology
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• v.26 no.5
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• pp.532-538
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• 1994

In order to investigate the lowering effects of in vitro enzymatic hydrolysis by the treatment of chymotrypsin, trypsin, pancreatin, or protease from Aspergillus oryzae on the antigenicity of whey protein(WPI) against rabbit anti ${\beta}-LG$ antiserum, competitive inhibition ELISA(cELISA) and passive cutaneous anaphylaxis(PCA) test using guinea pig were performed. The results of cELISA showed that the monovalent antigenicity of the whey protein hydrolysates(WPH) to the antiserum was decreased to $10^{-1.7}{\sim}10^{-4.1}$ and less by the hydrolysis. Especially, the antigenicity of OUP(hydrolysate by protease from Asp. oryzae with preteatment of pepsin) was found almost to be removed. By the heterologous PCA the polyvalent antigenicity of the WPH was decreased to $1/2{\sim}1/128$ and less. Especially, the polyvalent antigenicity of OUN(hydrolysate by protease from Asp. oryzae without preteatments) was found almost to be removed, although OUN did not have so high degree of hydrolysis(DH) or so low monovalent antigenicity (reduced to $10^{-3.2}$). Therefore, this result was assumed to come from effective destruction of antigenic determinants on ${\beta}-LG$ in WPI, not to produce polyvalent antigenic peptides that are closely associated with induction of allergy. This finding suggested that WPH prepared by the treatment of microorganic protease from Asp. oryzae would be a material for hypoallergenic infant formula due to the removal of the polyvalent antigenicity of ${\beta}-LG$, the major milk allergen in WPI.

• Applied Biological Chemistry
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• v.38 no.5
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• pp.468-472
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• 1995

Substantial amount of caryophyllene oxide (CPO) is present in the essential oils of traditionally-used folk medicinal plants and herbal spices. The CPO, produced via chemical and/or enzymatic reaction of caryophyllene (CP), has largely being used as a flavoring component and exhibited a variety of biological activities. Now, we report the antimutagenic activity of CPO determined by Ames's preincubation test. S-9 fraction was prepared from the liver of rats treated with Arochor 1254. Anatoxin $B_1\;(AFB_1)$ and 2-amino-3-methylimidazo[4,5-f]quinoline (IQ) were used as mutagens. Reduction of mutagenicity of $AFB_1$ or IQ for S. typhimurium TA98 and TA100 by CPO was found to be a dose-dependant manner. CPO (500 ${\mu}g/plate$) reduced mutagenicity of AEB1 for S. typhimurium TA98 and TA100 to 89% and 71%, respectively. For IQ, similar results were observed against S. typhimurium TA98 and TA100, resulting in the inhibition percentage of 77% and 51%, respectively. CP also reduced mutagenicity of AEB1 and IQ for S. typhimurium TA98 and TA100, but the reduction rate was somewhat lowered relative to that of CPO. These results indicate that CPO could be developed as a potent antimutagenic flavoring agent.

• Applied Biological Chemistry
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• v.50 no.2
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• pp.95-100
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• 2007

The cellulase gene of Bacillus licheniformis K11 which has plant growth-promoting activity by auxin and antagonistic ability by siderophore was cloned in pUC18 using PCR employing heterologous primers. The 1.6kb PCR fragment contained the full sequence of the cellulase gene, denoted celW which has been reported to encode a 499 amino acid protein. Similarity search in protein data base revealed that the cellulase from B. licheniformis K11 was more than 97% identical in amino acid sequence to those of various Bacillus spp. The cellulase protein from B. licheniformis K11, overproduced in E. coli DH5${\alpha}$ by the lac promoter on the vector, had apparent molecular weight of 55 kDa upon CMC-SDS-PAGE analysis. The protein not only had enzymatic activity toward carboxymethyl-cellulose (CMC), but also was able to degrade insoluble cellulose, such as Avicel and filter paper (Whatman$^{\circledR}$ No. 1). In addition, the cellulase could degrade a fungal cell wall of Phytophthora capsici. Consequently B. licheniformis K11 was able to suppress the peperblight causing P. capsici by its cellulase. Biochemical analysis showed that the enzyme had a maximum activity at 60$^{\circ}C$ and pH 6.0. Also, the enzyme activity was activated by Co$^{2+}$ of Mn$^{2+}$ but inhibited by Fe$^{3+}$ or Hg$^{2+}$. Moreover, enzyme activity was not inhibited by SDS or sodium azide.

• Journal of the Korean Society of Food Science and Nutrition
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• v.34 no.8
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• pp.1265-1273
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• 2005

The purpose of this study was to prepare accelerated salt-fermented anchovy sauce using a shrimp processing byproducts (head, shell and tail) as a fermenting accelerator, and to investigate its physicochemical and enzymatic properties. Four types of sauces were prepared with 0, 10, 20, and 30$\%$ (w/w) addition of shrimp byproduct and fermented at 24$\pm$2$^{\circ}C$ for 360 days. During fermentation, all four type sauces decreased moisture content (67.5$\%$68.0$\%$ to 64.0$\∼$64.8$\%$) and pH (5.52$\∼$7.10 to 5.03$\∼$6.58), but showed increase in their crude protein (7.0$\∼$8.2 to 10.8$\%$) and volatile basic nitrogen contents (40$\∼$75 to 180$\∼$200 mg/100 g of sauce). The ratio of amino nitrogen to total nitrogen contents of control (0$\%$) and sauce with 10$\%$ shrimp byproducts (10$\%$ sauce) were maximized at 270 days, whereas 20$ \% $ and 30$\%$ added sauces were at 180 days. Endoprotease and exoprotease activities of anchovy sauces added with 20$\%$ and 30$\%$ of shrimp byproducts tend to be higher than those of control (0$\%$) and 10$\%$ addition. Proteolytic activities of sauces at pH 9 were about 2 times higher than those at pH 6. Amidolytic activities for LeuPNA decreased remarkably during fermentation, and control (0$\%$) almost lost their activity at 180 days, while additional sauces were relatively stable. These suggest that alkaline pretense of anchovy and shrimp byproducts as a endoprotease mainly contributed to the fermentation of salt-fermented sauces. The protein molecular weight distribution of sauces indicated 2 groups of peaks (peak 1,>70,000 da and peak 2, 3,000$\∼$29,000 da). As the fermentation proceeded, peak 1 tended to decrease in all of sauces, but peak 2 increased rapidly from 30 to 270 days. Optimum fermentation periods of control and 10$\%$ sauces were 270 days and those of 20$\%$ and 30$\%$ sauce were 180 days. The results suggest that shrimp byproduct can be used as accelerator of salt-fermented sauce.

• Korean Journal of Food Science and Technology
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• v.30 no.3
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• pp.630-637
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• 1998

Enzymatic properties of immobilized transglucosidase (TG) from Aspergillus niger was characterized and compared with soluble TG. Michaelis-Menten constant $(K_m)$ and maximum velocity $(V_{max})$ of immobilized TG were $122\;mM,\;3.9{\times}10^{-2}\;mM/min$ and in case of soluble TG, 21 mM, 0.4 mM/min. The optimum pH of immobilized TG was pH 5.0 like soluble TG but immobilized TG showed 16% and 45% higher activity than soluble TG at pH 5.0 and pH 6.0. Both of immobilized TG and soluble TG were stable from pH 2.0 to pH 9.0, and therefore their activities in these pH ranges were remained more than 90%. The temperature was optimal at $60{\sim}70^{\circ}C\;and\;70{\sim}80^{\circ}C$ for soluble TG and immobilized TG, respectively. The thermal stability of immobilized TG was significantly improved than that of soluble TG, and immobilized TG retained $32{\sim}40%$ higher activity than soluble TG. D-values from thermal inactivation of immobilized TG were 7690 sec at $65^{\circ}C$, 83 sec at $75^{\circ}C$, 7.2 sec at $80^{\circ}C$. Z-values of soluble and immobilized TG were $6.4^{\circ}C\;and\;5.3^{\circ}C$, respectively. The little difference of activation energies of soluble TG and immobilized TG supposed that there was little difference in mass transfer limitation during the reaction of soluble TG and immobilized TG.

• Journal of the Korean Society of Food Science and Nutrition
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• v.17 no.3
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• pp.198-204
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• 1988

This study was aimed at obtaining elementary data on enzymatic browning of potato and potato products and examining the inhibitory method of browning. Therefore, we extracted polyphenol oxidase from potatoes(Solanum tubersum L.), and investigates its general properties and inhibiting effects of its activity with the different concentrations of sulfites($Na_2S_2O_4,\;Na_2SO_3{\cdot}7H_2O,\;NaHSO_3$). The optimum pH and temperature of polyphenol oxidase were observed to be 6.5 and $37^{\circ}C$ respectively. The polyphenol oxidase at PH5 was very stable, and the activity of polyphenol oxidase between pH $5.0{\sim}9.0$ was estimated to be relatively high, showing $72{\sim}75%$ of its activity at pH5. The polyphenol oxidase was very stable when heated at $40^{\circ}C$ for one hour, and almost 50% of enzyme activity was decreased when heated at $70^{\circ}C$ for twelve minutes. At 0.1mM concentrating of sulfites the relative activity of polyphenol oxidase was 98% in all the three cases of sulfites. Thus sulfites at 0.1mM concentration was found to have little inhibiting effect on polyphenol oxidase activity. At 1mM concentration of sulfites $NaHSO_3$ showed the lowest 36% relative activity among the three. At 5mM concentration of sulfites, the relative activity of $Na_2SO_3{\cdot}7H_2O$ was the lowest 14%.

• Journal of the Korean Society of Food Science and Nutrition
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• v.14 no.2
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• pp.164-170
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• 1985

Yellowish modified wool, dithiocarbamate(DTC) wool, was synthesized by partial hydrolysis in 0.2 N-NaOH reacting with carbon disulfide to use as ${\alpha}-amylase$ immobilization matrix. ${\alpha}-amylase$ was immobilized reacting with sulfide group of DTC-wool by covalent binding within 1 hour. 0.5 gram of this preparation, $DTC-wool-{\alpha}-amylase$, contained 150 ug of enzyme protein and its specific activity was about 90% of the native one. General properties of $DTC-wool-{\alpha}-amylase$ were a little different from optimum temperature, optimum pH, heat stability, kinetic constants and activation energy. An apparent Michaelis constant and maximum velocity of $DTC-wool-{\alpha}-amylase$ were 5.56 mg/ml and 0.37 mg/ml. $min^{-1}$ respectively, while activation energy was 16.6 kcal/mole.

• Journal of Korean Society of Forest Science
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• v.43 no.1
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• pp.31-34
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• 1979

In this study, enzymatic hydrolysis of the substrate of the waste wood of Cortinellus edodes was investigated using crude cellulase preparation of Trichoderma viride Pers. ex. Fr. SANK 16374. The crude cellulase was produced by the submerged culture process and produced in the culture fluid was salted out quantitatively by the use of ammonium sulfate. Reducing sugar was determined by the dinitrosalisylic acid (DNS) method. 1. The chemical composition of the waste wood was crude protein 2.26%, c. fat 2.57%, c. fibre 44.60%, c. ash 5.58% and lignin 13.62%. In amino acid composition, no cystine and methionine was showed, but trace amount of Vitamin A, $B_1$, and $B_2$, niacine and chloride were detected. (Table 1) 2. As heat treatment of the substrate was found to produce the highest reducing sugar yield being reacted for 48hr. with T.v cellulase, the substrate was heated to $190{\pm}5^{\circ}C$. for 45 min. either before or immediately after milling. 3. The substrate heated and ball milled at $190{\pm}5^{\circ}C$. for 45 min. the reducing sugar yield reached to 11.5%. 4. The substrate without any treatment was found to produce the highest reducing sugar yield being reacted 72hr. with T. v cellulase, the reducing sugar yield reached to 10.1%. 5. The rate of reducing sugar per each treated substrate was decreased by the order of the substrated, heated and then ball milled at $190{\pm}5^{\circ}C$. for 45 min. (11.5%)> without any treatment (10.1)> ball milled and heated at $190{\pm}5^{\circ}C$. for 45 min. (6.9%). 6. Saccharification of waste wood has been shown to be possible by heat treated and milling the substrate in contact with cellulase. And it is likely to be recommended that the waste wood may be valuable for raw materials of saccharification.

• Journal of the Korean Society of Food Science and Nutrition
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• v.36 no.10
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• pp.1326-1333
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• 2007

For preparing the basic ingredients of Gomtang-like products from the extracts of salmon frame, the extraction conditions of salmon frame were examined, and the characteristics of the extracts were compared with commercial Gomtang. Based on the crude protein, Ex-N and sensory attributes, the extractions were optimized by extracting pretreated-salmon frame in 12 times (v/w) of water for 12 hrs, before filtering with cheese cloth to yield 3 times the volume of the raw material. The concentrations of heavy metals in extracts from salmon frame were below the safety limits suggested by KFDA. The mai or amino acids were glutamic acid and aspartic acid as the free amino acids, and glycine, proline, and glutamic acid as the total amino acids. The calcium and phosphorus contents were 18.0 mg/100 mL and 33.1 mg/100 mL, respectively, and they accounted for 20% and 18% of the recommended daily allowance for mineral intake. The angiotensin I converting enzyme (ACE) inhibitory activity was improved by incubation with Flavourzyme for 4 hrs and its $IC_{50}$ was 2 mg/mL. The results above suggested that the enzymatic hydrolysates from extracts of salmon frame could be used as a basic ingredient for preparing Gomtang-like products.

• Food Science and Preservation
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• v.21 no.2
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• pp.163-169
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• 2014

The effect of the combined argon (Ar) gas packaging treatment on the browning of fresh-cut potatoes was studied. Fresh-cut potatoes were prepared for the following six groups: dipping distilled water for 1 minute and air packaging (Cont); dipping in distilled water for 1 minute and argon gas packaging (AR); dipping in 1% ascorbic acid for 1 minute and air packaging (AA); dipping in 1% ascorbic acid for 1 minute and argon gas packaging (AAR); blanching at $35^{\circ}C$ for 30 minutes and air packaging (BL); and blanching at $35^{\circ}C$ for 30 minutes and argon gas packaging (BAR). The potatoes were washed, peeled, and sliced ($1.5{\times}1.5{\times}1.5$ cm) before treatment. The samples were packed with a 0.04-mm-thick OPP film and were stored at $5^{\circ}C$ for 9 days. During the storage, the $O_2$ concentration decreased in Cont but increased in the AR, AA, AAR, BL, and BAR groups. The $CO_2$ concentration increased during storage. The AR, AAR, and BAR groups showed high $L^*$ and low $a^*$, $b^*$ values (browning index). The growth of the total aerobic bacteria was also inhibited in the AR group. During storage, the PPO activity gradually increased, and the AR group showed lower PPO activity. The AA and AAR groups showed high DPPH radical scavenging activity. It was demonstrated that the argon gas packaging is effective in the quality maintenance of fresh-cut potatoes.