• Journal of the Korean Society of Food Science and Nutrition
• /
• v.17 no.3
• /
• pp.242-248
• /
• 1988

Plasteins were synthesized from a peptic sardine protein hydrolysate by pepsin, ${\alpha}-chymotrypsin$ pretense(from Aspergillus saitoi) and papain under the optimum conditions of previous paper. L -glutamic acid diethylester and L-leucine ethylester also were incorporated into plastein during the plastein reaction by papain. General composition, yield, molecular weight and amino acid composition were measured. The protein, ash and lipid rontent of plasteins were $81.1{\sim}88.2%$, $1.9{\sim}7.6%$ and $0.3{\sim}0.8%$, respectively. The yield of plasteins were pretense plastein 52.3%, papain plastein 44.2%, pepsin plnstein 43.6%, ${\alpha}-chymotrypsin$ plastein 43.2%. Leu -papain plastein 33. 2% and Glu - papain plastein 29.0%. The glutamic acid and leucine content in Glu -papain plastein and Leu -papain plastein were 39.0%, 37.5%, respectively. While the contents in the papain plastein were 14.3%, 7.1%, respectively. The amino acid composition of plasteins were similar to that of peptic sardine protein hydrolysate. The major molecular weight of the peptic hydrolysnte estimated by gelfilteration were 1,800 and 285, and those of plasteins were 26,000 and 9,100 for ${\alpha}-chymotrypsin$, 23,000, 10,000 and 4,300 for pepsin, 18,000 for pretense, 13,000 for papain, 29,000 for Leu -papain plastein and 19,000 for Glu -papain plastein.

• KSBB Journal
• /
• v.21 no.5
• /
• pp.394-400
• /
• 2006

When the papain, which is a sort of Cystein protease, is applied to the outer skin, it decomposes the protein which forms the peeled outer skin and speeds up metabolism. Therefore, it is one of the most important cosmetics compositic which keeps the function of skin normal. When the papain is used in cosmetics with surfactant, the activity of papain is reduced rapidly. In this study, the modified papain with extreme stability negative ionic environment was developed by directed evolution

• Journal of Sericultural and Entomological Science
• /
• v.29 no.2
• /
• pp.58-66
• /
• 1987

This study was investigated on the effect of degumming of cocoon shell, raw silk yarn and grey silk crepe by use of Papain, comparing with soap, soda and soap-soda. The obtained results may be summarized as follows : 1. Degumming loss, when the pretreatment was done, was completed by Papain more than by alkali. 2. Lousiness result of Papain degummed silk yarn was apt to be improved more than that of alkali degummed one. 3. As a result of tensile property test, elasticity and resilience of Papain degummed crepe were good compared to those of alkali degummed one. 4. Not only bending rigidity of Papain degummed crepe was reduced more than that of alkali degummed one but also hysteresis of bending moment was decreased in papain degummed crepe. 5. Handle of Papain degummed crepe was superior to that of alkali degummed one.

• Fashion & Textile Research Journal
• /
• v.16 no.2
• /
• pp.333-338
• /
• 2014

This study identifies the effects of sodium sulfate and surfactants in the papain treatment of wool fabrics using L-cysteine and EDTA as activators. The research method involves the use of 2% L-cysteine and 7% EDTA as activators at optimal conditions, papain treatment of wool fabrics with the joint use of sodium sulfates and surfactants, and measurements of the weight loss rate, tensile strength, and whiteness. Results showed that for both 2% L-cysteine and 7% EDTA, the maximum papain activity appeared at 0.5% sodium sulfate concentration. In both cases, the papain activity was enhanced at sodium sulfate concentrations lower than 0.5%. In contrast, the papain activity declined at sodium sulfate concentrations higher than 0.5%. The joint use of EDTA with 0.5% sodium sulfate was proven to be very effective in improving the papain activity. The joint use of 2% L-cysteine with 0.5% sodium sulfate appeared slightly effective in improving the activity but resulted in excessive decrease in the tensile strength and whiteness, compared to improvement in the activity. The joint use of surfactants, in the case of L-cysteine, interrupted the papain activity and decreased the tensile strength regardless of the surfactant type and concentration. In the case of EDTA, however, the joint use with 0.1-5% non-ionic surfactants, 0.1-0.5% anionic surfactants, and 0.1% cationic surfactant appeared to improve the papain activity. The maximum papain activity was observed when 0.1% of surfactant was used, regardless of the surfactant type. The nonionic surfactant was the most effective in improving the papain activity.

• Journal of the Korean Society of Clothing and Textiles
• /
• v.33 no.2
• /
• pp.213-221
• /
• 2009

This study provides the optimum papain treatment method and its effect on wool/polyester blend fabrics. The enzymatic treatment condition is optimized depending on its pH level, temperature, concentration of enzyme, treatment time and concentration of activators. The characteristics of samples treated with the papain are measured using weight loss, tensile strength, whiteness, WCA, dyeing property and surface micrographs. The results are described as follows: According to measuring weight loss, tensile strength and whiteness, a pH level of 7.5, $70^{\circ}C$, 10% papain(o.w.f.) and 60minutes of treatment time are optimized for papain treatment. L-cysteine and sodium sulfite are able to activate the papain. The optimum concentrations of them are 10mM and 50mM respectively. The WCA of fabrics is decreased since papain treatment makes wool/polyester blend fabrics more hydrophilic. Scouring with papain treatment improves whiteness and dyeing property of fabrics. The dyeing property of papain-treated fabrics is enhanced simply by a single step dyeing process using a basic dye. The surface of wool treated with papain in the presence of L-cysteine shows to be descaled. The surface of wool fibers in the presence of sodium sulfite, however, shows it is hydrolyzed evenly instead of being descaled. The surface of papain treated polyester fibers shows cracks and voids.

• The Korean Journal of Food And Nutrition
• /
• v.20 no.4
• /
• pp.349-355
• /
• 2007

Periodate-oxidized soluble starch was reacted with papain at pH 4.0, pH 7.0, and pH 9.7, and an oxidized soluble starch-papain conjugate was produced. When compared with native papain, the specific activity decreased to 60%, in both the modified papain reacted with 0.4% $NaBH_4$ and in the modified papain not reacted with $NaBH_4$. The specific activity decreased to 70% in the modified papains reacted with 1.5% $NaBH_4$ and 4.0% $NaBH_4$, respectively. The reduction by $NaBH_4$ did not have an effect in the thermal stability of either the modified or nonmodified papain. An activity of 54.7% remained in the papain modified at pH 4.0, which was incubated at $80^{\circ}C$ for 40 min. The papains modified at pH 7.0 and pH 9.7 and incubated for 40 min at two different temperatures, respectively, were stable to $60^{\circ}C$, and at $80^{\circ}C$ their activities at 56.3% and 44.1 %, respectively. The modified papain's thermal stability pattern was similar to that of native papain, with no increase in its statbility. In the range of pH $2.0{\sim}13.0$, the stability of the papain modified at pH 4.0 decreased greatly between pH $3.0{\sim}5.0$, but it was similar to the native papain at other pH values. The stability of the papain modified at pH 7.0 showed a similar pattern to the native papain at pH $2.0{\sim}6.0$, while its stability increased when moving into the alkali pH range. The papain modified at pH 9.7 also had increased stability, when moving into the alkali range. The results of Hammerstein milk casein, which was reacted with the papains modified at pH 4.0, pH 7.0, and pH 9.7, respectively, and analyzed by FPLC, showed different peaks according to the different modification pHs, and the greatest peak differences were observed with the modification at pH 9.7.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.17 no.4
• /
• pp.312-319
• /
• 1988

The functional properties of plasteins have been compared with those of sardine protein concentrate and egg albumin. The solubility of plasteins was higher than that of FPG and the glu-plastein had 84% solubility in the range of pH 3-10. The dispersibility of plasteins was lower than that of egg albumin, however those of plasteins was higher than that of sardine protein concentrate. The water holding capacity of plasteins was higher than that of egg albumin. Lipid absorption of leu-papain plastein was the highest, holding 2.2m119, and that of the other plastein was higher than that of egg albumin. The emulsifying activity of leu-papain plastein was the highest, holding 66.4%, and that of glu-papain plastein was the lowest, holding 51.2%, The emulsifying stability of plasteins was similar to that of the emulsifying activity. The foaming capacitt of leu-papain plastein was the highest, holding 460%, and those of the other plasteins was higher than that of egg albumin. The foaming stability of plasteins was superior to that of egg albumin. The viscosity of plasteins was lower than that of see albumin. The in vitro digestibility of plasteins was 67.6-78.0% range. The digestibility by four pretense were somewhat lower in the glu-papain plastein than in the FPG. The digest of plasteins treated with the microbiol pretense such as molsin and pretense(from Streptomyces griceus), which had a storage broth taste.

• Korean Journal of Food Science and Technology
• /
• v.29 no.3
• /
• pp.509-515
• /
• 1997

Crude papain was extracted from papaya latex under various conditions. Extraction conditions of crude papain were optimized by the response surface methodology (RSM). Extraction yield of papain was affected by concentration of $NaHSO_3$, extraction time and pH. Three independent factors were chosen to determine their effects on the various responses and the function was expressed in terms of a quadratic polynomial equation, which measures the linear, quadratic and interaction effects. According to the results of RSM, the stationary point for quantitatively dependent variable was found to be the maximum point for extraction yield. Optimum conditions of papain extraction were 4% of $NaHSO_3$, 120 min of extraction time and pH 7.6. Under these conditions, 793.16 mg of papain per g latex was extracted from papaya latex.

• Journal of the Korean Society of Clothing and Textiles
• /
• v.34 no.4
• /
• pp.697-702
• /
• 2010

This study researches the mechanical and dyeing properties of wool fabric treated with papain. In this study, shrinkage, water contact angle, alkali solubility, and the dyeability of wool fabric treated with papain at the optimal activity condition were measured to confirm the effect of papain treatment. The shrinkage and water contact angle of wool fabric treated with papain decreased more than the untreated wool; however, the alkali solubility and the dyeability increased. L-cysteine was more active than EDTA as an activator of papain.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.20 no.6
• /
• pp.582-590
• /
• 1987

Plasteins were synthesized from a peptic filefish protein hydrolysate by papain, $\alpha-chymotrypsin$ and protease(from Streptomyces griceus) under the optimum conditions of previous paper. L-glutamic acid diethylester and L-leucine ethylester were incorporated into plastein during the plastein reaction by papain. The structural changes of freeze-dried filefish meat, peptic hydrolysate, FPC and plasteins were observed by Scanning Electron Microscopy(SEM). The functional properties of plasteins also were measured. The solubility of plasteins was higher than that of FPC and the Glu-plastein had $95\%$ solubility in the range of pH 3-10. The dispersibility of Glu-plastein and protease plastein was similar to that of egg albumin, but those of the other plasteins were lower. The water holding capacity of plasteins was lower than that of egg albumin and C. Lipid absorption of Leu-plastein was tile highest, holding 1.80 ml/g, and that of the other plasteins was similar to that of egg albumin. The emulsifying activity of Leu-plastein was the highest, holding $61.2\%$, and that of Glu-plastein was the lowest, holding $50.7\%$. The emulsifying stability of plasteins was similar to that of the emulsifying activity. The emulsifying capacity of Leu-plastein was 384 ml/g(the highest), but that of Glu-plastein and $\alpha-chymotrypsin$ plastein was 248 ml/g(the lowest). The Leu-plastein shelved the highest foaming capacity, $373\%$. The foaming capacity of other plasteins was higher than that of egg albumin. The foaming stability of plasteins was superior to that of egg albumin. The viscosity of plasteins was lower than that of egg albumin. The microstructure of $\alpha-chymotrypsin$ plastein by SEM wassimilar to that of papain plastein, but other plasteins showed differences in their microstructure. The microstructure of Glu-plastein had a smooth shape.