• Journal of the Society of Cosmetic Scientists of Korea
• /
• v.33 no.2
• /
• pp.93-97
• /
• 2007

Even in the moderately concentrated anionic surfactant system, some special encapsulation method can shield the papain enzyme from proteolytic attacks. The stabilization of enzyme has been a major issue for successful therapies. In this study, we first stabilized an enzyme, papain in the microcapsules by using polyols, polyethyleneglycol (PEG), poly-propyleneglycol (PPG), and PEG-PPG-PEG block copolymer. In the analysis of EDS and CLSM, it was demonstrated that polyols are effectively located in the interface of papain and polymer. Polyols located in the interface had an ability to buffer the external triggers by hydrophobic partitioning, preventing consequently the catalytic activity of papain in the micro-capsules. Second. we introduced multi-layer capsulation methods containing ion complex. Such a moderately concentrated anionic surfactant system as wash-off cleansers, surfactants and waters can cause instability of entrapped enzymes. Surfactants and water in our final products swell the surface of enzyme capsules and penetrate into the core so easily that we can not achieve the effect of enzyme, papain. In this case, the ion complex multi-layer capsule composed of sodium lauroyl sarcosinate and polyquaternium-6 could effectively prevent water from penetration into the core enzyme, followed by in vivo test, and evaluate the stratum corneum (SC) turn-over speed.

• Textile Coloration and Finishing
• /
• v.20 no.2
• /
• pp.9-18
• /
• 2008

Wool has excellent properties, such as heat retention, absorbency, and elasticity, but it has a disadvantage in washability because the fabric will felt and shrink greatly. Felting causes the interlocking of the fiber surface scales with one another. Therefore, the studies on wool finishing have been focused on shrink proofing. Precedent researches on wool shrink proofing are mostly on eco-friendly method. using enzyme. The purpose of this study is to examine the effect of L-cysteine, EDTA in papain treatment of wool fabrics. The specific contents of study are as follows. Depending on pH, temperature, treatment time, enzyme concentration and L-cysteine, EDTA concentration, weight loss, tensile strength, whiteness, SEM were examined. Each papain treatment conditions depending on L-cysteine, EDTA were optimized from these properties. Papain had very low activation without activators. The optimum conditions of papain treatment were pH 7.5, temperature $75^{\circ}C$, time 30minutes(L-cysteine), 180minutes(EDTA) and papain concentration 5%(o.w.f.). In the use of papain 5%(o.w.f.), the activators optimum concentration was L-cysteine 2%(o.w.f.), EDTA 7%(o.w.f.)

• 한국생물공학회:학술대회논문집
• /
• 2000.04a
• /
• pp.347-350
• /
• 2000

Enzymatic deinking of office-waste paper was studied using crude cellulase and papain-hydrolyzed cellulase from Trichoderma reesei Rut C-30 in small-scale and mid-scale. The results were compared with deinkings using commercial enzyme(Novozym 342) and conventional chemical methods. Maximum brightness and freeness were obtained at 3 units/g Oven Dry Paper(ODP) of CMCase activity using crude cellulase in mid-scale deinking experiments. The deinked pulp had higher physical strength and brightness, and lower freeness and yield than the pulp deinked in small scale. In small scale deinking, maximum brightness and freeness were obtained at 2 unit/g ODP. Deinking by papain-hydrolyzed cellulase showed similar results with one by Novozym 342. It was better in brightness and freeness, but showed lower physical strength and yield, than the conventional deinking by sodium hydroxide. The ratio of endo-1,4-glucanase and exo-1,4-glucanase components in papain hydrolyzed cellulase from T. reesei Rut C-30 was similar to that of commercial enzyme, Novozym 342, implicating a successful application as a deinking enzyme.

• Journal of the Korean Society of Clothing and Textiles
• /
• v.32 no.9
• /
• pp.1461-1466
• /
• 2008

This study provides effects of mixed activators on enzymatic activation and determines optimum mixture ratio for enzymatic treatment. Wool 80% and polyester 20% blend fabric and papain from carica papaya are used in this experiment. L-cysteine and sodium sulfite are used as activators for papain treatment process. The treatment condition is pH 7.5, $70^{\circ}$, papain concentration 10%(o.w.f), 60 minutes. L-cysteine and sodium sulfite are added in enzyme solution with various concentrations($0{\sim}50mM$). The optimum treatment condition is determined by measuring weight loss, tensile strength, whiteness, water contact angle(WCA), dyeability and surface micrographs. The results are as follow; The optimum mixture ratio of activators is L-cysteine 2mM and sodium sulfite 10mM. Mixed activators assists in improving the activation of papain. WCA of papain treated fabrics is decreased since papain treatment with activator mixture makes wool polyester blend fabrics more hydrophilic. Dyeing property of papain-treated fabrics more improves by the treatment with mixed activators than with single activator. It means that this method can save time and lower cost. After papain treatment in the presence of mixed activator, the surface of fabrics is modified. The surface of wool fiber shows to be descaled and hydrolyzed, and that of polyester fiber shows to be cracked.

• Korean Journal of Fisheries and Aquatic Sciences
• /
• v.20 no.4
• /
• pp.282-292
• /
• 1987

In order to exploit a new type of food source, enzamatically modified hydrolysates and the plasteins synthesized from the filefish (Nevoden modestus) protein hydrolysates by plastein reaction were investigated. The optimum conditions for enzymatic hydrolysis of filefish muscle and synthesis of plasteins using papain, pepsin, $\alpha-chymotrypsin$ and protease (from Streptomyces griceus) were determined. The optimum temperature and pH for the hydrolysis of filefish muscle by papain, pepsin, $\alpha-chymotrypsin$ and protease were $50^{\circ}C,\;40^{\circ}C,\;55^{\circ}C\;and\;50^{\circ}C$; and 6, 2, 7 and 8, respectively. Those for incubation time and enzyme concentration were 4hr, $0.5\%$ for papain and protease, 24hrs $1.0\%$ for pepsin and $\alpha-chymotrypsin$. The pepsin was found to be more reasonable substrate for plastein synthesis from the economic point of view. The enzyme-induced plastein reaction could be optimized, namely, pH 4 for pepsin, pH 7 for $\alpha-chymotrypsin$, pH 6 for papain and protease: substrate concentration $40\%$ for pepsin, $\alpha-chymotrypsin$ and protease, $50\%$ for papain; the time of incubation, 24hr; enzyme/substrate ratio, 1 : 100(W/V) ; incubation temperature, $50^{\circ}C$.

• Applied Biological Chemistry
• /
• v.30 no.3
• /
• pp.234-241
• /
• 1987

Conditions necessary for optimal plastein productivity from sardine protein hydrolysate using papain and pepsin were established. Sardine protein concentrate was hydrolyzed with pepsin yielding an approximate degree of hydrolysis of 77.2%. Enzyme induced plastein was optimized at: pH 6 for papain and pH 4 for pepsin; substrate concentrate, 50%(w/v) for papain and 40%(w/v) for pepsin; time of incubation, 24hr; enzyme/substrate ratio, 1 : 100(w/w). Plastein yields of 49.5% and 45.3% were found for papain and pepsin, respectively, when 10% trichloroacetic acid (TCA) was used as the precipitating agent. However, when plastein was precipitated by 50% ethanol, the yield was found to be 43.6% and 41.0% for papain and pepsin, respectively. Ethanol-precipitated plastein did not contain lipid and contained approximately 1.3% ash and 91.0% protein. In comparison, the TCA-precipitated plastein contained 74.2% protein, 0.5% lipid and 15.3% ash.

• Journal of the Society of Cosmetic Scientists of Korea
• /
• v.26 no.1
• /
• pp.81-92
• /
• 2000

Development of stabilized enzyme was attempted for cosmetic applications. Papain, a proteolytic enzyme, was stabilized through conjugation with a soluble carbohydrate biopolymer, SC-glucan$^{TM}$ . With a novel structure of the conjugation site, stability of the enzyme was significantly enhanced such that more than 90% of the initial activity retained after a month storage at 45$^{\circ}C$, while no activity were detected in native enzyme or enzyme simply mixed with SC-glucan$^{TM}$ after the storage. Conjugation with SC-glucan$^{TM}$ not only extended the half-life of the enzyme on storage at higher temperature, but was also found to protect enzymes against some components contained in cosmetic products for skin care. Cosmetic lotion containing 1 % papain conjugate was more effective and less irritative in exfoliating stratum corneum of human skin than the lotion containing 5% lactic acid, one of the current popular exfoliating agents.gents.

• 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

• Food Science of Animal Resources
• /
• v.41 no.4
• /
• pp.608-622
• /
• 2021

Bioactive peptides have great potentials as nutraceutical and pharmaceutical agents that can improve human health. The objectives of this research were to produce functional peptides from ovotransferrin, a major egg white protein, using single enzyme treatments, and to analyze the properties of the hydrolysates produced. Lyophilized ovotransferrin was dissolved in distilled water at 20 mg/mL, treated with protease, elastase, papain, trypsin, or α-chymotrypsin at 1% (w/v) level of substrate, and incubated for 0-24 h at the optimal temperature of each enzyme (protease 55℃, papain 37℃, elastase 25℃, trypsin 37℃, α-chymotrypsin 37℃). The hydrolysates were tested for antioxidant, metal-chelating, and antimicrobial activities. Protease, papain, trypsin, and α-chymotrypsin hydrolyzed ovotransferrin relatively well after 3 h of incubation, but it took 24 h with elastase to reach a similar degree of hydrolysis. The hydrolysates obtained after 3 h of incubation with protease, papain, trypsin, α-chymotrypsin, and after 24 h with elastase were selected as the best products to analyze their functional properties. None of the hydrolysates exhibited antioxidant properties in the oil emulsion nor antimicrobial property at 20 mg/mL concentration. However, ovotransferrin with α-chymotrypsin and with elastase had higher Fe³⁺-chelating activities (1.06±0.88%, 1.25±0.24%) than the native ovotransferrin (0.46±0.60%). Overall, the results indicated that the single-enzyme treatments of ovotransferrin were not effective to produce peptides with antioxidant, antimicrobial, or Fe³⁺-chelating activity. Further research on the effects of enzyme combinations may be needed.

• Korean Journal of Food Science and Technology
• /
• v.6 no.3
• /
• pp.163-168
• /
• 1974

Authors investigated the tenderness effect of beef which was treated with papain and obtained results indicated as follow. 1. By using the sensory test, most desirable tenderness were obtained in 0.05% of enzyme solution for 40minute to 1 hour at $25^{\circ}C$. 2. It was also somewhat recognized as a tenderness effect with treated for 40minute to 1 hour at $10^{\circ}C$. 3. Water soluble and amino acid nitrogen were increased in proportion to enzyme concentration, reaction temperature and reaction time and opposite in connective tissue nitrogen. 4. It will be recognized that there were correlation between result of sensory test and water soluble, amino acid and connective tissue nitrogen.