• Journal of Sericultural and Entomological Science
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• v.42 no.1
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• pp.48-57
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• 2000

This study was undertaken to figure out the effects of hydrolysis conditions on the solubility of insoluble sericin, molecular weight distribution and thermal characteristics of hydrolysates in enzymatic hydrolysis by Alcalase 2.5L. It was indicated that the optimum treatment temperature and pH for the insoluble sericin were 50$\^{C}$ and 11, respectively. When the insoluble sericin was hydrolyzed with a various treatment conditions, the solubility of all hydrolysates were represented above 85% at given conditions. As the enzyme concentration increased, the solubility increased roughly, but the solubility increasement ratio was less above 2% enzyme concentration. As the treatment time increased, the solubility was also increased. It was showed in the molecular weight distribution of hydrolysates treated various enzyme concentrations and treatment times that when enzyme concentrations were 0.5, 2, 3%, the peaks of the distribution curve were shifted to left side which meant low molecular weight and was distributed much quantity with shifted to be left side, but treatment time was 6 hr. the peak was shifted to right side. When enzyme concentration was 5% and treatment time was below 2 hr., the peaks were shifted to right side, but treatment time was above 4hr. the peak was shifted to left side. The number-average molecular weights were distributed from 300 to 800 and those were decreased when treatment time was up to 4 hr., but increased a little when treatment time was 6hr. It was showed in the DSC curves of hydrolysates treated with treatment time of 0.5, 1, 2, 4, 6 hr. fixed 1% o.w.s enzyme concentration and control that the endothermic peak was observed near at 200$\^{C}$. The denaturation peak of the hydrolysates depending on treatment times had a tendency to shift to higher temperature. But, when the treatment time was 6 hr., the peak was shifted to lower temperature comparing another hydrolysates.

• KSBB Journal
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• v.10 no.5
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• pp.540-546
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• 1995

Dry corn gluten meal of 70% protein content was enzymatically hydrolyzed by alkaline protease in a pH-state reactor. Such process variables as temperature, pH, and enzyme-to-substrate ratio were varied, and at each condition degree of hydrolysis was monitored and calculated. The ultimate degree of hydrolysis, which ranged between 25 and 28% based on gluten protein mass, was not significantly affected by the process variables. However, $50^{\circ}C$ and pH 9-10 appeared optimum. Kinetic analysis indicated enzyme deactivation was negligible during the hydrolysis, and the experimental data were near perfectly fitted to the model kinetic equation which was modified after neglecting enzyme deactivation term. The enzyme reaction was 1$100\times$ scaled up and basically the same hydrolysis performance was resulted. Amino acid analysis showed the hydrolyzate was relatively rich in glutamine/glutamic acid, leucine, and alanine at 19.6, 16.1, and 12.3 mole %, respectively.

• 한국생물공학회:학술대회논문집
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• 2000.11a
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• pp.504-507
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• 2000

Enzymatic hydrolysis of cellulose was studied with emphasis on the effect of cellulase loading and pulp sludge concentration on glucose yield. Enzyme loading appeared to have a significant effect on glucose yield. Chemical pretreatment had no effect on enzymatic hydrolysis of pulp sludge. High glucose yield was obtained from enzymatic hydrolysis, especially at sludge concentrations lower than twenty percent. The optimum concentrations of crude cellulase and ${\beta}-glucosidase$ were 5 U/mL and 8 U/mL, respectively, considering the amount of enzymes used and glucose produced.

• The Korean Journal of Food And Nutrition
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• v.8 no.2
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• pp.79-87
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• 1995

It is generally known that the protein of talk has allergenicity and the allerenicity Induces allergic diseases. Finding methods to reduce the allergenicity of the food and develop methods to make low allergic food is the purpose of this study. For this study, 1 tried various experimental methods : heat treatment, irradation with ultraviolet and microwaves treatment with polyphosphate, enzyme hydrolysis and PCA inhibition test using guinea pigs and degrees of hydrolysis. The results obtained are as follows. Heat treatment reduced allergenicity of milk protein. The higher the heat, the better the effect. Irradiating with ultraviolet and microwave increased both the degree of protein hydrolysis and PCA inhibition reduced the allergenicity. Ultraviolet was more effective than microwaves on milk protein. Enzyme treatment increased the degree of hydrolysis and PCA inhibition, and reduced allergenicity considerably. Neutrase was more effective than alcalase on milk protein. Adding Polyphosphate did not induced protein hydrolysis, but increased PCA inhibition and reduced allergenicity.

• Food Science and Biotechnology
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• v.16 no.3
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• pp.482-484
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• 2007

To investigate production and hydrolysis of levan, the levansucrase enzymes from Zymomonas mobilis ATCC 10988 and Rahnella aquatilis ATCC 33071 were used. The optimum temperature of R. aquatilis levansucrase for levan formation was $37^{\circ}C$, whereas that of Z. mobilis was $4^{\circ}C$, under the experimental conditions. Both levansucrases also catalyzed the reverse levan hydrolysis reaction. Levan hydrolysis reactions from both levansucrases were temperature dependent; high temperature ($20^{\circ}C$) was more favorable than low temperature ($4^{\circ}C$) by 4 times. Fructose was the only product from hydrolysis reaction by both levansucrases, showing that both levansucrases mediated the hydrolysis reaction of exo-enzyme acting. In both enzymes, initial levan hydrolysis activity was almost accounted to 1% of initial levan formation activity. The results allow the estimation of the fructose release rate in enzyme processing conditions.

• Korean Journal of Food Science and Technology
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• v.50 no.2
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• pp.203-208
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• 2018

In this study, the hydrolysis conditions for the production of anti-inflammatory peptides from meat and roe hydrolysates of sandfish (Arctoscopus japonicus) were determined by measuring the nitric oxide (NO) scavenging enzymatic activity, experimental pH, temperature, enzyme concentration, and hydrolysis time. The optimal conditions determined when using meat hydrolysate were a pH value of 5.0, at a temperature of $30^{\circ}C$, 1% enzyme concentration, and 4 h hydrolysis time. The optimal conditions when using roe hydrolysate were a pH of 5.0, a temperature of $70^{\circ}C$, enzyme concentration of 3%, and hydrolysis time of 3 h. The NO scavenging activities of meat and roe hydrolysate were determined to be 18.94 and 19.81%, respectively. In summary, this study determined the optimum enzymatic hydrolysis conditions for the production of anti-inflammatory peptides from sandfish.

• Journal of Life Science
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• v.17 no.9 s.89
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• pp.1260-1265
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• 2007

Magnetically separable enzyme-coated nanofibers were developed for the hydrolysis of starch. Stability of ${\alpha}-amylase-coated$ nanofiber was greatly improved and its residual activity was maintained over 92.7% after 32 days incubation at room temperature and under shaking conditions (200 rpm). The recovery of enzyme was high and enzyme activity after 10 recycle was 95.2% of its original activity. Developed enzyme-coated nanofibers were used for the hydrolysis of starch. When 0.5 mg of magnetically separable enzyme nanofibers was used, 40 g/l of starch (2 ml) was completely degraded within 40 min. The continuous enzyme reactor was developed and used for starch hydrolysis and 76% of starch (30 g/l) was hydrolyzed with 1 hr residence time.

• Journal of Ginseng Research
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• v.40 no.2
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• pp.105-112
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• 2016

Background: Minor saponins or human intestinal bacterial metabolites, such as ginsenosides Rg3, F2, Rh2, and compound K, are more pharmacologically active than major saponins, such as ginsenosides Rb1, Rb2, and Rc. In this work, enzymatic hydrolysis of ginsenoside Rb1 was studied using enzyme preparations from cultured mycelia of mushrooms. Methods: Mycelia of Armillaria mellea, Ganoderma lucidum, Phellinus linteus, Elfvingia applanata, and Pleurotus ostreatus were cultivated in liquid media at $25^{\circ}C$ for 2 wk. Enzyme preparations from cultured mycelia of five mushrooms were obtained by mycelia separation from cultured broth, enzyme extraction, ammonium sulfate (30-80%) precipitation, dialysis, and freeze drying, respectively. The enzyme preparations were used for enzymatic hydrolysis of ginsenoside Rb1. Results: Among the mushrooms used in this study, the enzyme preparation from cultured mycelia of A. mellea (AMMEP) was found to convert ginsenoside Rb1 into compound K with a high yield, while those from G. lucidum, P. linteus, E. applanata, and P. ostreatus produced remarkable amounts of ginsenoside Rd from ginsenoside Rb1. The enzymatic hydrolysis pathway of ginsenoside Rb1 by AMMEP was $Rb1{\rightarrow}Rd{\rightarrow}F2{\rightarrow}$ compound K. The optimum reaction conditions for compound K formation from ginsenoside Rb1 were as follows: reaction time 72-96 h, pH 4.0-4.5, and temperature $45-55^{\circ}C$. Conclusion: AMMEP can be used to produce the human intestinal bacterial metabolite, compound K, from ginsenoside Rb1 with a high yield and without food safety issues.

• Journal of Microbiology and Biotechnology
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• v.6 no.6
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• pp.407-413
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• 1996

A novel type of extracellular phospholipase $A_1$ was isolated from Serratia sp. MK1 and purified to homogeneity by ammonium sulfate precipitation, anion exchange and gel filtration chromatography. The purified enzyme was a monomer with a molecular mass of about 43, 000 Da. This enzyme showed the highest lipolytic activity toward phosphatidylserine among the phosphoglycerides tested, and preferentially catalyzed the hydrolysis of the ester bond in phosphatidic acid to lyso-phosphatidic acid. Enzyme activity was completely inhibited by the addition of a chelating agent such as EDTA, and inhibited enzyme activity was fully recovered by the presence of $Ca^{2+}$. This implies that the enzyme requires $Ca^{2+}$ for activity. The enzyme was stable up to $70^{\circ}C$ when incubated for 1 h at pH 8.5, and the optimal pH and temperature were 8.5 and $50^{\circ}C$, respectively.

• Proceedings of the Korean Society for Applied Microbiology Conference
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• 1986.12a
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• pp.525.2-525
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• 1986

Cephalexin synthesizing enzyme (${\alpha}$ amino acid ester hydrolase) was partially purified from the culture broth of Acetobacter turbidans ATCC9325 through ammonium sulfate fractionation, DEAE, CM, and Sephacryl S-200 gel filtration. The enzyme has optimum pH 6.0 and temperature, 40$^{\circ}C$ respectively. From the analysis of reaction mixtures by thin layer chromatographic and high performance liquid chromatographic techniques, it was confirmed this enzyme catalyzed simultaneously the following reactions : 1) Synthesis of cephalexin from D-${\alpha}$-phenylglycine methylester (PGM) and 7-amino 3-deacetoxy-cetoxycephalosporanic acid (7-ADCA) 2) Hydrolysis of cephalexin to form 7-ADCA and phenylglycine (PG) 3) Hydrolysis of PGM to form PG and methanol. Base on the above experimental observations, the reaction model of this enzyme was identical with that of the enzyme from Xanthomonas citri.