• Title/Summary/Keyword: Papain

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Glyceryl Esterification of Fibroin Peptide by Papain (파파인을 이용한 피브로인 펩타이드의 글리세릴 에스터화 반응)

  • Jeong, Jae-Ho;Lee, Shin-Young;Hur, Won
    • KSBB Journal
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    • v.25 no.4
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    • pp.395-400
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    • 2010
  • Papain hydrolysate of fibroin was found to be mainly composed of several even-numbered peptides that can be produced at a large scale and can be used as a precursor for biological fine-chemicals such as peptide detergents. Thus, the hydrolysate was further modified to synthesize a peptide mixture of glyceryl esters using the identical enzyme for the production of such chemicals. Formation of glyceryl ester of each peptide was confirmed by identifying peaks of the nominal mass shift of +74 Da in mass spectrometry. Analysis of the mass spectra indicated that glyceryl esters of di- and tetra-peptides were the major constituents of the mixture and that alanylglycine was most preferentially esterified. It also suggests that papain prefers dipeptide to tetrapeptide and alanine to serine or tyrosine at $P_2$ position as substrate for glyceryl esterification. The glyceryl esters were recovered using ion exchange resin and the yield of glyceryl esterification recorded was 17.8% by weight.

Studies on the Aging of Beef at Adding the Proteolytic Enzyme -VI. Effects of Papain Treatment on the Enzymatic Digestibility of Beef- (단백질(蛋白質) 분해효소(分解酵素) 첨가시(添加時) 우육(牛肉)의 숙성(熟成)에 관(關)한 연구(硏究) -VI. Papain처리(處理)가 우육(牛肉)의 소화율(消化率)에 미치는 영향(影響)-)

  • Youn, Jung-Eae
    • Korean Journal of Food Science and Technology
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    • v.10 no.4
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    • pp.394-397
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    • 1978
  • In vitro digestibility study using pepsin was conducted on round muscle previously treated with papain and the change in the amounts of liberated amino nitrogen was followed during the time course of digestion procedure. The obtained results were summarized as follows. 1. As compared with control, enzyme treatment groups had higher digestibility and curtailed digestion time. 2. All the enzyme treatment groups showed the highest digestibility between 6 and 10 hours in the course of digestion procedure. 3. The amounts of liberated amino nitrogen were increased similarly to digestibility and digestion time. 4. As compared with control, enzyme treatment groups showed considerably higher amounts of liberated amino nitrogen, the liberation rate being the highest between 2 and 8 hours of digestion time.

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Studies on the Aging of Bovine Muscle at Adding the Proteolytic Enzyme -VII. Studies on the Histological Observation of Bovine Muscle Treated with Papain- (단백질(蛋白質) 분해효소(分解酵素) 첨가시(添加時) 우육(牛肉)의 숙성(夙成)에 관(關)한 연구(硏究) -VII. Papain 처리(處理) 우육(牛肉)의 조직학적(組織學的) 고찰(考察)-)

  • Yoon, Jung-Eui
    • Korean Journal of Food Science and Technology
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    • v.9 no.4
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    • pp.271-276
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    • 1977
  • Treating with step concentration of papain, round mucle of Korean cattle were cut in longitudinal and cross section and stained. Collagenous fibre and elastic fibre of its connective tissue were observed microscopically. The results were as follows: 1) In proportion to the increase of enzyme concentration amorphous bundle of collagenous fibre were loosed gradually and destroyed in the long run and besides the property of this fibre stained became remarkably weak. 2) Elastic fibre was paralleled to muscle fibre and in proportion to the increase of enzyme concentration, it was lost elasticity, loosed, straightened and broken remarkably to pieces. 3) Histological variation of collagenous fibre and elastic fibre treated with enzyme was more remarkable than control.

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Stabilization of Enzyme in "Solvophobically" Controlled Polymer Microcapsules ("솔보포빅"한 고분자 마이크로 캡슐을 이용한 효소 안정화에 관한 연구)

  • Kim, Yong-Jin;Kim, Jin-Woong;Kim, Jin-Oh;Kim, Jin-Woo;Chang, Ih-Seop
    • Journal of the Society of Cosmetic Scientists of Korea
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    • v.32 no.1 s.55
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    • pp.29-33
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    • 2006
  • This article describes an enzyme stabilization method that allows the use of enzymes irrespective of environmental factors, especially heat, while maintaining their activity for a long time. We have designed enzyme microcapsules that consist of papain enzyme cores, poly(propylene glycol) interlayers, and poly(${\epsilon}-caprolactone$) walls. By confocal laser scanning microscopy measurements and the thermal stability of papain-loaded microcapsules, it is demonstrated that the papain is surrounded by a hydrophobic polyol layer and stabilized by the exclusive volume effect. In our study, improved thermal stability can be obtained by using more hydrophobic long-chained polyols, which is understood to be attributed to the effective formation of a hydrophobic polyol layer between the papain and the polymer wall by means of conformational anchoring in the interface.

Effect of Vigna angularis Ethanol Extract on Papain-induced Arthritis in Mice (팥 에탄올 추출물의 Papain 유도 관절염 마우스에서의 항 골관절염 효과)

  • Jeoung, See Hwa;Kim, Seung Hyung;Kim, Hyun Kyu;Yun, Bo Ra;Lee, Hee Woong;Lim, Ju Hwan;Rho, Mun Chual;Kim, Dong Hee
    • Journal of Physiology & Pathology in Korean Medicine
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    • v.26 no.5
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    • pp.665-671
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    • 2012
  • The purpose of this study is to examine the effect of Vigna angularis ethanol extract (VA-E) on papain induced arthritis in C57BL/10 mice. The C57BL/10 mice were injected with papain and oral administration of Vigna angularis ethanol extract (VA-E) at different doses (100 and 200 mg/kg) once a day for 42 days and compared with untreated mice. Histological examination and the measurement of inflammatory cytokine release were performed. The results showed that comparing with untreated mice, the treatment with Vigna angularis ethanol extract (VA-E) decreased the pathological changes of knee joint tissue. The level of inflammatory cytokine secreted from the tissues, such as IL-$1{\beta}$ (interleukin-$1{\beta}$), IL-6 (interleukin-6), TNF-${\alpha}$ (Tumor Necrosis Factor-${\alpha}$), were decreased. These results were confirmed by the quantification of cartilage volume using micro CT scanning. Consequently, Vigna angularis ethanol extract (VA-E) has a therapeutic potential in inflammatory joint diseases such as osteoarthritis.

Studies on the Aging of Bovine Muscle at Adding Proteolytic Enzyme -Part V. Studies on the Tenderness Evaluation of Bovine Muscle Treated with Papain by Using Penetration Value- (단백질(蛋白質) 분해효소(分解酵素) 첨가시(添加時) 우육(牛肉)의 숙성(熟成)에 관(關)한 연구(硏究) -제5보 Papain처리(處理) 우육(牛肉)의 Penetration Value에 의한 유연성(柔軟性) 평가(評價)에 관(關)하여-)

  • Youn, Jung-Eae;Yang, Ryung
    • Korean Journal of Food Science and Technology
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    • v.7 no.4
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    • pp.208-211
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    • 1975
  • Round muscle of Korean cattle treated with papain were examined the tenderness relation by use of penetrometer which results were indicated as follows. 1. Measuring method of tenderness effect in bovine muscle was acknowledged that there are correlation by using penetrometer (p<.05) 2. Penetration value were also proportional increased according to increasing of enzyme concentration. 3. It was acknowledged as considerable difference in penetration value cf longitudinal and cross section against muscle fiber. 4. In the case of 0.05% enzyme addition, there are extremely high increasing rate of tenderness in longitudinal and cross section but it was not acknowledged as significant difference in 0.1% of enzyme concentration.

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Enzymatic Hydrolysis of Ovotransferrin and the Functional Properties of Its Hydrolysates

  • Rathnapala, Ethige Chathura Nishshanka;Ahn, Dong Uk;Abeyrathne, Edirisingha Dewage Nalaka Sandun
    • Food Science of Animal Resources
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    • v.41 no.4
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    • pp.608-622
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    • 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.

Antioxidative Activities of Hydrolysates from Duck Egg White Using Enzymatic Hydrolysis

  • Chen, Yi-Chao;Chang, Hsi-Shan;Wang, Cheng-Taung;Cheng, Fu-Yuan
    • Asian-Australasian Journal of Animal Sciences
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    • v.22 no.11
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    • pp.1587-1593
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    • 2009
  • Duck egg white (DEW) hydrolysates were prepared by five enzymes (papain, trypsin, chymotrypsin, alcalase, and flavourzyme) and their antioxidant activities investigated in this study. DEW hydrolyzed with papain (DEWHP) had the highest peptide content among the five enzymatic treatments. Besides, the peptide content of DEWHP increased when the enzyme to substrate ratio (E/S ratio) increased. It was suggested that higher E/S ratio contributed to elevate the degree of hydrolysis of DEW effectively. Similar results were also obtained by Tricine-SDS-PAGE. In addition, SDS-PAGE patterns indicated papain was the only one amongst all enzymes with the ability to hydrolyze DEW. In antioxidant properties, DEWHP showed more than 70% of inhibitory activity on linoleic acid peroxidation and superoxide anion scavenging. Moreover, the $Fe^{2+}$ chelating effect of DEWHP was greater than 90%, while no significant difference was observed in DPPH radical scavenging and reducing ability. The results of peptide contents, antioxidant activities and electrophoresis suggested that the higher the peptide content, the stronger the antioxidant activities in DEWHP.

Freezing Preservation of Liquid Egg by Freezing Point Depression (빙점강하에 의한 액란의 냉동저장에 관한 연구)

  • Lee, Young-Chun;Lee, Kyung-Hae
    • Korean Journal of Food Science and Technology
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    • v.20 no.4
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    • pp.594-599
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    • 1988
  • Methods by which liquid egg could be stored in liquid state at frozen storage temperature$(-15^{\circ}C)$ with selected cryoprotectants and enzyme treatment were investiated, and quality changes in samples during storage were examined. The concentration of cryoprotectants (45% fructose and 55% glucose) to be added to egg yolk and whole egg to store them at $-15^{\circ}C$ in unfrozen state were 45.2% and 70.3%, respectively. Changes in consistency, precipitation of protein and microstructure of egg samples during storage indicated that adding cryoprotectants to liquid egg could effectively inhibit development of gelation during storage at $-15^{\circ}C$. Treating liquid egg with 0.15% papain could inhibit gelation during storage to some extent.

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Optimal Conditions for the Enzymatic Hydrolysis of Isolated Sesame Meal Protein (효소에 의한 참깨박 단백질의 최적 가수분해 조건)

  • Lee, S.H.;Cho, Y.J.;Kim, S.;Ahn, B.J.;Choi, C.
    • Applied Biological Chemistry
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    • v.38 no.3
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    • pp.248-253
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    • 1995
  • Optimum conditions for the enzymatic hydrolysis of isolated sesame meal protein were investigated. Optimum conditions by papain were $60^{\circ}C$, pH 6.0, 3% enzyme concentration to substrate and 1.5% substrate concentration, respectively. The optimum operating conditions using pepsin were $55^{\circ}C$, pH 9.0, 3% enzyme concentration to substrate and 1% substrate concentration. The optimum operating conditions using trypsin were $60^{\circ}C$, pH 9.0, 1% enzyme concentration to substrate and 1% substrate concentration.

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