• Title, Summary, Keyword: pepsin activity

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Effect of Linoleate Hydroperoxide on Pepsin Activity (리놀레산 과산화물이 펩신 활성도에 미치는 영향)

  • Choi, Kap-Seong;Kim, Ze-Uook;Moon, Tae-Wha
    • Korean Journal of Food Science and Technology
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    • v.23 no.2
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    • pp.224-228
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    • 1991
  • The effect of linoleate hydroperoxides(LAHPO) on pepsin activity was investigated. The activity of pepsin was largely decreased by LAHPO at various temperatures and pH. The inactivation of pepsin seems to be the radicals in the system because ascorbate and metal ions enhanced the inactivation of enzyme by LAHPO. It was shown by SDS-PAGE that LAHPO caused scission of the enzyme in the model system.

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A Study on Changes in Antibacterial Activity of Pepsin-hydrolyzed Bovine Apo-lactoferrin at Various Method for Pasteurizations and pH Values (살균방법 및 pH 조건에 따른 Pepsin-hydrolyzed Bovine Apo-lactoferrin의 항균성 변화에 관한 연구)

  • 김종우;이조윤;금종수;유대열
    • Food Science of Animal Resources
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    • v.18 no.2
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    • pp.157-163
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    • 1998
  • This study was carried out to examine that pepsin-hydrolyzed bovine lactoferrin has applicabilities which are market milk and dairy products. The stability of pepsin-hydrolyzed bovine apo-lactoferrin and the change of its antibacterial character has been studied under various method for pasteurization (LTLT; 65$^{\circ}C$ / 30min., HTST ; 75$^{\circ}C$ / 15sec., UHT ; 135$^{\circ}C$ / 3sec.) and pH Values (pH 2.0, pH 4.0, pH 6.8). The ehated samples were assayed for minimal bacteriocidal concentrations (MBCs) and bacteriocidal effect against E. coli. The results obtained were summarized as follows: After fractionation of pepsin-hydrolyzed bovine lactofeerin by gel filtration. several peptide fractions were found that had strong antibacterial activity. SDS-PAGE showed that the one of these fractions with strong antibacterial activity, which had a molecular mass a range of 30∼33KDa. The MBCs for pepsin-hydrolyzed bovine lactoferrin fraction No. 2 against E. coli required to cause complete inhibition of growth varied within the range of 200∼400 $\mu\textrm{g}$/ml, depending on heat treatments and pH conditions. The peptide fraction No. 2 showed strong bacteriocidal activity against E. coli at LTLT and HTST treatments under acidic pH conditions. and was reduced activity at UHT treatment under pH 6.8 condition.

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The Effect of Synthetic Antioxidants on the proteolytic Enzymes-The Effect of Synthetic Antioxidants on the Activity of the Pepsin and Synthesis of Octapeptide as a Substrate- (합성 항산화제가 단백질 분해효소에 미치는 영향-Pepsin의 활성에 미치는 합성 항산화제의 영향 및 기질 Octapeptide의 합성-)

  • Kim, Sang-Ock
    • Journal of Nutrition and Health
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    • v.14 no.3
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    • pp.124-128
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    • 1981
  • This study was carried out to understand the activity of pepsin, the proteolytic enzyme, to octapeptide (angiotensin II) in the presence of various synthetic antioxidants as food additives. 1) Dibutyl hydroxy toluene, butyl hydroxyanisole and ethyl protocathechuate did not influence the inhibitory activity of pepsin an the octapeptide as a substrate, but sodium-L-ascorbate inhibited pepsin activity at above 100ppm. However sodium L-ascorbate was completely removed after 30 minutes. 2) Pepsin brought about a quick break up the octapeptide, Asp-Arg-Val-Tyr-Ile-His-Gly-Phe, by splitting the Gly-Phe and Val-Tyr bond. 3) The melting point of synthetized octapeptide was $209-212^{\circ}C$, chemical formula and molecula weight were $C_{43}H_{65}N_{13}O_{12}{\cdot}CH_3COOH{\cdot}H_2O$ and 956.05, respectively. 4) The amino acid mole ratio of synthetized octapeptide by acid hydrolysis were Asp:0.98, Arg: 1.02, Val: 1.00. Tyr: 0.95, Ile: 1.00, His: 1.03, Gly: 0.96, Phe: 1.00.

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The Changes of Digestive Enzyme Activity in Early Stages of the River Puffer, Takifugu obscurus (황복, Takifugu obscurus, 초기 단계의 소화효소 변화)

  • SON Kyu-Hee;HAN Kyung-Nam;CHANG Chung-Soon
    • Korean Journal of Fisheries and Aquatic Sciences
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    • v.34 no.6
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    • pp.577-583
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    • 2001
  • The digestive enzyme activities such as $\alpha-amylase$, trypsin and pepsin from the laboratory-reared river puffer Takifugu obscurus were measured from the time course of 1 day until the 65 day after hatching. In the case of $\alpha-amylase$, it was showed minimum activity of 0.0493 U/mg at the total length (TL) 10 mm, and showed maximum activity of 0.1480 U/mg at 19 mmTL. Trypsin and pepsin were showed their maximum activities of 0.0264, 0.0258 U/mg and 0.0178, 0.0201 U/mg when the total length of 16 and 24 mm, and represented remarkable correlations between the changes of enzyme activity and growth rate. The ontogenetic variations of digestive enzymes were represented clearly different patterns; i.e, the pepsin showed higher activity when the periods of larva ($4\~5\;mmTL$) and juvenile II ($19\~24\;mmTL$), however, the trypsin represented maximum activity at the stages of juvenile I ($11\~16\;mmTL$) and young fish (27 mmTL), respectively.

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Effect of High Pressure on the Porcine Placenral Hydrolyzing Activity of Pepsin, Trypsin and Chymotrypsin

  • Chun, Ji-Yeon;Jo, Yeon-Ji;Min, Sang-Gi;Hong, Geun-Pyo
    • Food Science of Animal Resources
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    • v.34 no.1
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    • pp.14-19
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    • 2014
  • This study investigated the effects of protease treatments (trypsin, chymotrypsin, and pepsin) under various pressure levels (0.1-300 MPa) for the characteristics of porcine placenta hydrolysates. According to gel electrophoretic patterns, the trypsin showed the best placental hydrolyzing activity followed by chymotrypsin, regardless of the pressure levels. In particular, the peptide bands of tryptic-digested hydrolysate were not shown regardless of applied pressure levels. The peptide bands of hydrolysate treated chymotrypsin showed gradual decreases in molecular weights ($M_w$) with increasing pressure levels. However, the pepsin did not show any evidences of placental hydrolysis even though the pressure levels were increased to 300 MPa. The gel permeation chromatography (GPC) profiles showed that the trypsin and pepsin had better placental hydrolyzing activities under high pressure (particularly at 200 MPa), with lower $M_w$ distributions of the hydrolysates. Pepsin also tend to lower the $M_w$ of peptides, while the major bands of hydrolysates being treated at 300 MPa were observed at more than 7,000 Da. There were some differences in amino acid compositions of the hydrolysates, nevertheless, the peptides were mainly composed of glycine (Gly), alanine (Ala), hydroxyproline (Hyp) and proline (Pro). Consequently, the results indicate that high pressure could enhance the placental hydrolyzing activities of the selected proteases and the optimum pressure levels at which the maximum protease activity is around 200 MPa.

A Study on Immoblization of Pepsin (��프신의 고정화(固定化)에 관한 연구(硏究))

  • Park, Jong Lae
    • Current Research on Agriculture and Life Sciences
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    • v.3
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    • pp.166-173
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    • 1985
  • Several enzyme immobilization methods has been compared for immobilization of pepsin. Carboxymethyl cellulose and diethylaminoethyl cellulose were activated with Hcl and with NaOH, and were used for immobilization of pepsin. Sepharose-4B was activated cyanogen bromide, and was used for immobilization of pepsin. Porous glass beads were derivatized with 3-aminopropyitrlethoxysilane and with succinicanhydride, and were used for immobilization of pepsin. The results abtained were summarized as follow, 1. 10 mg/gr. dry bead and 15mg/gr. dry bead of pepsin were absorbed to CM-cellulose and DEAE-cellulose, 20 mg/gr. dry bead and 27 mg/gr. dry bead were coupled to CM-cellulose and DEAE-cellulose with glutaraldehyde respectively. Enzyme yields were 22% and 24% of soluble pepsin. 2. 16 mg/gr. dry bead of pepsin was attached to cyanogen bromide activated sepharose-4B, 19mg/gr. dry bead was cross linked to the activated bead with glutaraldehyde. Immobilized enzyme activity was 23% of soluble pepsin. 3. 40 mg/gr. dry bead of pepsin was conjugated to the derivatized glass beads. Immobilized enzyme activity was 45% of soluble pepsin.

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Developmental Changes in Digestive Organ and Digestive Enzyme Activity of Filefish Thamnaconus modestus (말쥐치 Thamnaconus modestus 자치어의 성장에 따른 소화기관 및 소화효소 발달)

  • Gwak, Woo-Seok;Lee, So-Gwang
    • Korean Journal of Ichthyology
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    • v.21 no.3
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    • pp.149-157
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    • 2009
  • Larvae and juveniles of the filefish Thamnaconus modestus were reared for 64 days after hatching (DAH) in order to determine the activity of four enzymes (trypsin, pepsin-like enzyme, lipase, amylase) during ontogeny. Larvae were fed on rotifer Brachionus plicatilis from 2 to 26 DAH, Artemia nauplii from 10 to 64 DAH, and then gradually changed to pelleted feed from 40 DAH. Temperature was kept between $21.5{\sim}24.2^{\circ}C$ Activity of trypsin and lipase was found in larvae 4 DAH ($6.0{\pm}1.4unit$) and 6 DAH ($4.5{\pm}1.4unit$), respectively. The evolution of activity in both enzymes showed a profile marked by drastic increases between late larval and early juvenile stages. Pepsin-like enzyme activity was found at 10 DAH and drastically increased from 28 DAH, corresponding with the early juvenile stage of T. modestus. Interestingly, developmental changes in the pepsin-like enzyme activity coincided well with increases in the number of gastric glands. Amylase activity was found at 10 DAH and was maintained at a low level up to 28 DAH, followed by a drastic increase from 28 DAH to 40 DAH. It might be concluded that a drastic increase in trypsin and pepsin-like enzyme activities, and a corresponding increase in the number of gastric glands reflects a higher somatic growth of T. modestus during the early juvenile period.

Antibacterial Activity of Zein Hydrolysate with Pepsin (Pepsin에 의한 Zein 가수분해물의 항균활성)

  • Kang, Yoon-Jung;Yi, Sang-Duk;Lee, Gyu-Hee;Oh, Man-Jin
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.35 no.2
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    • pp.127-131
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    • 2006
  • A study was carried out to produce antimicrobial peptides from zein treated with pretenses of six kinds. Among the pretenses of six kinds, zein hydrolysate treated with pepsin showed the highest antimicrobial activity. The zein hydrolysate with pepsin was fractionated with membrane filter (30,000 10,000 and 3,000 molecular weight cut-off) and antimicrobial activity was measured for each fractions. Antimicrobial activity appeared greatly in the fraction below 3,000 (molecular weight cut-off) . The fraction was re-fractionated by HPLC and substances of two peaks collected as a sample to measure antimicrobial activity. All of both peaks showed the antimicrobial activity but 1st peak exhibited a consistently higher antimicrobial activity than 2nd peak. Minimum inhibitory concentrations (MIC) were between 2.5 and 3.0 mg/mL. The peptide was heat-stable since antimicrobial activity was maintained after treated with heat for 20 min at $121^{\circ}C$. N-terminal amino acid sequence of peptide fractionated by HPLC was leucine, glutamic acid, proline, phenylalanine, aspartic acid and argenine. These results indicated that peptide isolated from zein hydrosate with pepsin can use as a natural preservative ingredient in food industry.

Isolation and Screening of Pepsin Inhibitor-Producing Actinomycetes (Pepsin 저해물질을 생산하는 방선균의 분리 및 검색)

  • 박석규;성낙계;노종수
    • Microbiology and Biotechnology Letters
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    • v.17 no.2
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    • pp.115-120
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    • 1989
  • For the purpose of obtaining microorganisms which produced an extracellular pepsin inhibitor, screening test was carried out. One strain of Actinomycetes (GF 155-2) isolated from soil samples showed a high inhibitory activity against porcine pepsin. The morphological, physiological and cultural characteristics of the strain GE 155-2 on various culture media were studied according to ISP methods and Bergey's manual of determinative bacteriology (8th ed.). This Actinomycetes GE 155-2 was found to be similar to the genus Microtetraspora.

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Antioxidant Activity of Porcine Skin Gelatin Hydrolyzed by Pepsin and Pancreatin

  • Chang, Oun Ki;Ha, Go Eun;Jeong, Seok-Geun;Seol, Kuk-Hwan;Oh, Mi-Hwa;Kim, Dong Wook;Jang, Aera;Kim, Sae Hun;Park, Beom-Young;Ham, Jun-Sang
    • Food Science of Animal Resources
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    • v.33 no.4
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    • pp.493-500
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    • 2013
  • Gelatin is a collagen-containing thermohydrolytic substance commonly incorporated in cosmetic and pharmaceutical products. This study investigated the antioxidant activity of gelatin by using different reagents, such as 2,2-azinobis-(3-ethylbenzothiazoline- 6-sulfonic acid) (ABTS), 2,2-di (4-tert-octylphenyl)-1-picrylhydrazyl (DPPH), and oxygen radical absorbance capacity-fluorescein (ORAC-FL) in a porcine gelatin hydrolysate obtained using gastrointestinal enzymes. Electrophoretic analysis of the gelatin hydrolysis products showed extensive degradation by pepsin and pancreatin, resulting in an increase in the peptide concentration (12.1 mg/mL). Antioxidant activity, as measured by ABTS, exhibited the highest values after 48-h incubation with pancreatin treatment after pepsin digestion. Similar effects were observed at 48 h incubation, that is, 61.5% for the DPPH assay and 69.3% for the ABTS assay. However, the gallic acid equivalent (GE) at 48 h was $87.8{\mu}M$, whereas $14.5{\mu}M$ GE was obtained using the ABTS and DPPH assays, indicating about sixfold increase. In the ORACFL assay, antioxidant activity corresponding to $45.7{\mu}M$ of trolox equivalent was found in the gelatin hydrolysate after 24 h hydrolysis with pancreatin treatment after pepsin digestion, whereas this activity decreased at 48 h. These antioxidant assay results showed that digestion of gelatin by gastrointestinal enzymes prevents oxidative damage.