• Journal of Sericultural and Entomological Science
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• v.42 no.2
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• pp.104-108
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• 2000

To hydrolyze insolule sericin the enzyme hydrolysis was used, and then obtained the results as given belows. When insoluble sericin was hydrolyzed by enzyme treatment, the solubility was best at pH 7, 60$\^{C}$ and was slightly increased both above 2 hours treatment and above 10% of enzyme concentration. As the results of electrophoresis, the distribution of molecular weight of sericin powder obtained by enzyme hydrolysis was very weak and showed in the wide range having no distinguishable band. Average degree of polymerzations (A.D.P.) of sericin hydrolyzed by enzyme were about 4.1∼6.3, average molecular weight were about 470∼730. The whiteness of the sericin powder obtained by enzyme hydrolysis was high and increased slightly with higher treatment concentration of enzyme. As the results of amino acid analysis, the amino acid analysis, the amino acid composition of the sericin powder from the enzyme treatment were similar to which located at near 230$\^{C}$ and 320$\^{C}$. The peak of near 230$\^{C}$ could not been found in the sericin powder obtained by enzyme hydrolysis.

• Journal of Sericultural and Entomological Science
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• v.42 no.1
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• pp.31-35
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• 2000

When insoluble sericin was hydrolyzed by treatment of NaOH solution, the solubility was increased with higher treatment temperature and longer treatment time. Whereas it was decreased in addition of NaHSO$_3$. As the results of electrophoresis in sericin powder obtained by the NaOH treatment, a distinguishable band was not confirmed. Average degree of polymerizations(A.D.P.) of sericin hydrolyzed by NaOH solutions were about 19.6∼22.1 and average molecular weight(M.W.) were about 2,200∼2,500. The longer hydrolysis time increased the whiteness of sericin powder. As the results of amino acid analysis, the contents of Thr., Tyr., and Ser. were decreased in NaOH hydrolysis as compared to HCl hydrolysis. In DSC analysis, thermal deformation and pyrolysis peak located at near 230$\^{C}$ and 320$\^{C}$, respectively.

• Membrane Journal
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• v.19 no.2
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• pp.145-149
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• 2009

The aim of this paper is to investigate removal of salts in hydrolyzed sericin solution by a prepared nanofiltration membrane. The nanofiltration membrane was prepared by the interfacial polymerization method, and then compared with commercialized nanofiltration membrane in terms of salts removal. The sericin solution was hydrolyzed by a protease. The molecular weight distribution of the hydrolyzed sericin was determined by electrophoresis method. Relative flux measurements were carried out to investigate membrane fouling.

• Journal of Sericultural and Entomological Science
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• v.45 no.1
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• pp.46-57
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• 2003

This study was carried out to investigate the characteristics of the soluble sericins after degumming and after hydrolysis of insoluble sericin with various enzymes. Especially, the hydrolysis characteristics were examined in terms of molecular weight of the soluble sericin. Amino acid composition and molecular weight characteristics of the soluble sericins were also studied. When the insoluble sericin was hydrolyzed with kojizyme and flavourzyme, the solubility was highest at pH 7 and 50$^{\circ}C$. On the other hand, in the cases of protamex and alcalase, the highest solubility was obtained at 60$^{\circ}C$. In these cases, solubility increased with pH. In enzymatic hydrolysis, the solubility was increased with concentration of enzymes until 4 hours. After then, a slight difference was found along with treatment times. In enzymatic hydrolysis, the absorbance of the soluble sericin was increased with concentration of enzymes and treatment times. Average degree of polymerization was decreased with treatment time and concentration. The amino acid compositions were similar in low(low molecular weight by degumming) and high (high molecular weight by degumming). Those of PK (soluble sericin hydrolyzed with kojizyme), PP (soluble sericin hydrolyzed with protamex), and PA(soluble sericin hydrolyzed with alcalase) were similar to each other. Serine and tyrosine compositions were higher in low and high than those of PK, PP, and PA. However proline was absent in low and high. Molecular weights of the various sericins became higher as KP>high>PP>low>PA and those of KP and PA were 9,800 and 905 respectively.

• Journal of Sericultural and Entomological Science
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• v.41 no.1
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• pp.48-53
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• 1999

The study was carried out to investigate the effects of hydrolysis conditions such as treatment times and concentrations on the solubility of insoluble sericin using the hydrochloric acid solution. When insoluble sericin was hydrolyzed by HCl solution, the solubility was increased with the higher treatment concentration. As the results of electrophoresis of sericin powder obtained by the HCl treatment, a distinguishable band was not confirmed. Average degree of polymerizations(A.D.P.) of sericin hydrolyzed by HCl solution were about 4.2~5.9 and average molecular weights(M.W.) were about 470~670. The longer hydrolysis time reduced the whiteness of sericin powder. As the results of amino acid analysis, the amino acid compositions of the sericin powder from HCl treatment were sililar to that of insoluble sericin, but Tyr. and Arg. were not detected in the powder obtained by HCl treatment. In DSC analysis, thermal deformation and pyrolysis peak located at near 220$^{\circ}C$ and 330$^{\circ}C$.

• Journal of the Society of Cosmetic Scientists of Korea
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• v.35 no.2
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• pp.135-141
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• 2009

In this study, we hydrolyzed hot-water extracted sericin with single or two enzymes and investigated anti-oxidative effect on DPPH free radical and inhibitory effect on tyrosinase activity of the sericin hydrolysates. Alcalase, flavourzyme, and protamex were effective in hydrolyzing sericin. Sericin was degraded into the range of 20 ${\sim}$ 30 kDa. The sericin hydrolysate was shown to have stronger antioxidant properties than the original sericin. In the case of flavourzyme and protamex combination, the scavenging effect of sericin hydrolysate on DPPH radical was increased up to about 85 %. However, the inhibitory effect on tyrosinase activity of enzymatic hydrolysates was lower than that of the original sericin. After fractionation of sericin hydrolysates, we found that F2 and P3 fraction has higher inhibitory effect on tyrosinase activity compared to other fractions.

• Journal of the Korean Chemical Society
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• v.20 no.4
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• pp.309-315
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• 1976

An efficient separation method and the utilization of sericin are searched. Sericin was extracted with hot water from cocoons under atmospheric pressure. The separated sericin was gel-filtrated with Sephadex G-75 and G-150 at room temperature and at $70^{\circ}C$. The results indicated that sericin is consisted of only one fraction in elution diagram. In the graft copolymerization of acrylonitrile to sericin ceric ammonium nitrate was chosen as an initiatior. A maximum yield was obtained at certain concentration of the initiator confirming our previous experiments. Viscosity measurement of alkali-hydrolyzed graft copolymers indicated that the polyacrylonitrile graft had the molecular weight in the range of 7,000.

• Journal of the East Asian Society of Dietary Life
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• v.20 no.5
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• pp.680-686
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• 2010

Silk sericin protein was hydrolyzed by seven proteolytic enzymes in order to examine the effectiveness of the hydrolysates in binding calcium. The amino acid nitrogen content of hydrolysates from Flavourzyme was higher than that for other enzymes, and its calcium binding capacity showed a dose-dependent increase. We examined the effects of calcium binding peptide from sericin hydolysates on the bioavailability of Ca-deficient rats. Three-week-old male rats were fed an Ca-deficient diet for three weeks. Rats were divided into four groups (DD: non-treated group on calcium deficient diet; DD+MC: milk-calcium treated group; DD+OC: organic calcium made using sericin hydolysates; and DD+IC: inorganic calcium ($CaCl_2$). After oral administration of calcium supplements for one week, the calcium content of the serum and liver were significantly higher in DD+OC ($101.7{\mu}g$/mL and $49.3{\mu}g$/mL) and DD+MC ($83.6{\mu}g$/mL and $42.8{\mu}g$/mL) than DD ($86.3{\mu}g$/mL and $43.4{\mu}g$/mL). The alkaline phosphatase (ALP) content in the treated groups was significantly lower than DD, but no significant difference among groups was shown. Aspartate aminotransferase (AST) levels did not show any significant difference between groups. Alanine aminotransferase (ALT) levels were significantly reduced compared to the DD group. In conclusion, binding calcium to peptides from sericin hydrolysates seems to improve its bioavailability, and to hasten the cure of calcium deficiency in experimental rats.

• 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.

• Journal of the Korean Society of Food Science and Nutrition
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• v.39 no.10
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• pp.1446-1451
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• 2010

Silk sericin protein was hydrolyzed by seven proteolytic enzymes to examine the effectiveness of the hydrolysates to bind iron. The amino acid nitrogen contents of hydrolysates by Flavourzyme were higher than the others enzymes, and its iron binding capacity showed dose-dependent increase. The bioavailability of iron binding peptide from sericin hydolysates was investigated in iron-deficient rats. Three-week-old male rats were fed iron-deficient diet for three weeks. Rats were divided into four groups (DD: no treated group on iron deficient diet, DD+HI: heme-iron treated group, DD+OI: sericin-Fe, and DD+II: inorganic iron ($FeSO_4$) treated group, and then iron supplemented by injection for one week. After oral administration for one week, the iron contents of serum and liver were significantly higher in DD+OI ($4.2\;{\mu}g/mL$ and $80.1\;{\mu}g/mL$) and DD+HI ($3.2\;{\mu}g/mL$ and $70.6\;{\mu}g/mL$) than DD ($2.0\;{\mu}g/mL$ and $47.9\;{\mu}g/mL$). Hemoglobin content of treated groups was significantly higher than DD, but the significant difference among groups was not shown. Aspartate aminotransferase (AST) and alanine aminotransferase (ALT) levels did not show any significant difference among all groups. Binding iron to peptide from sericin hydolysates seems to improve its bioavailability and to hasten the cure of iron deficiency in experimental rat.