• 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.

• 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.

• 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.

• 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.

• 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.

• 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.

• 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.

• Asian-Australasian Journal of Animal Sciences
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• v.16 no.3
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• pp.417-424
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• 2003

Inhibitory activities against angiotensin I-converting enzyme (ACE) of enzymatic hydrolysates of porcine skeletal muscle proteins were investigated. Myosin B, myosin, actin, tropomyosin, troponin and water-soluble proteins extracted from pork loin were digested by eight kinds of proteases, including pepsin, $\alpha$-chymotrypsin, and trypsin. After digestion, hydrolysates produced from all proteins showed ACE inhibitory activities, and the peptic hydrolysate showed the strongest activity. In the case of myosin B, the molar concentration of peptic hydrolysate required to inhibit 50% of the activity increased gradually as digestion proceeded. The hydrolysates produced by sequential digestion with pepsin and $\alpha$-chymotrypsin, pepsin and trypsin or pepsin and pancreatin showed weaker activities than those by pepsin alone, suggesting that ACE inhibitory peptides from peptic digestion might lose their active sequences after digestion by the second protease. However, the hydrolysates produced by sequential digestion showed stronger activities than those by $\alpha$-chymotrypsin, trypsin or pancreatin alone. These results suggested that the hydrolysates of porcine meat were able to show ACE inhibitory activity, even if they were digested in vivo, and that pork might be a useful source of physiologically functional factors.

• 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.

• Journal of the Korean Chemical Society
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• v.14 no.2
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• pp.161-168
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• 1970

In order to obtain the more effective evidence, supporting the hypothesis which have been previously described by former report that pepsin (EC 3.4. 4.1) forms a hydrophobic bond with the nonpolar side chain of its substrate, the inhibitory effect of carboxylic acids(from formic acid to iso-butyric acid) on the activity of pepsin to the synthetic dipeptide, N-Carbobenzoxy-L-glutamyl-L-tyrosine, was discussed. The kinetic study showed that the inhibition by carboxylic acids was competitive. The Kidecreased with increasing size of the inhibitor molecule. The $-{\Delta}F^{\circ}$increased linearly with increasing number of carbon atoms in the hydrocarbon chain of the inhibitor. It was confirmed that the hydrophobic bond between more than one side chain of amino acid residues(phenylalanine) in the binding region of the active center of pepsin and the side chain of amino acid residues in the substrate was formed as the first step of its enzymic mechanism. The inhibitory effect of carboxylic acids was due to the competition of the hydrocarbon group of the carboxylic acids with the side chain of the substrate for the hydrophobic binding site(the side chain of phenylalanine) of the pepsin.