• Korean Journal of Poultry Science
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• v.11 no.1
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• pp.13-17
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• 1984

Protein digestibitlities of hydrolyzed cattle skin meals were examined at a constant pepsin-MC$\ell$ concentration (0.2%) for varying lengths of incubation time (from 4 to 20 hours) and at varying concentrations of pepsin-HC$\ell$ (from 0.0125 to 0.2%) for 16 hours at 45$^{\circ}C$. The results are summarized as follows: 1. Protein digestibilities of hydrolyzed cattle skin meals in 0.2% pepsin-HCl were 66.31%, 80.69%, 83.72%, 84.65% and 81.45% for 4, 8, 12, 16 and 20 hours incubation, respectively. Protein digestibilities were maintained above 80% for 8-hour incubation and were increasing incubation time. 2. Protein digestibilities of hydrolyzed cattle skin meal incubated for 16 hours at 0.2%, 0.1%, 0.05%, 0.025% and 0.0125% pepsin-HC$\ell$ solution were 85.10%, 82.08%, 76.18%, 74.67% and 64.82%, respectively. Protein digestibilities were decreased with decreasing pepsin concentration.

• 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.

• 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.

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

• Microbiology and Biotechnology Letters
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• v.17 no.2
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• pp.121-125
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• 1989

Actinomycetes GF 155-2, which produced an extracellular pepsin inhibitor, was isolated from soil samples. Optimal conditions of inhibitor production by flask-shacking culture were 2% glucose, 0.7% polypeptone, initial pH 1.0, culture time 60 hours and temperature 30%. Effect of in-organic salts was not observed. About 5mg of colorless crystalline inhibitor was obtained from 5L culture broth in jar tormentor by means of ammonium sulfate precipitation, methanol extraction, and column chromatographies on Amberlite IR-120, XAD-2 and silicagel 60.

• 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.

• Journal of the Korean Chemical Society
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• v.14 no.2
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• pp.155-160
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• 1970

The kinetics of the pepsin-catalyzed hydrolysis of N-carbobenzoxy-L-glutamyl-L-tyrosine at pH 3.5 and $37^{\circ}C$ were determined by a spectrophotometric technique. The pepsin used was further purified on a Sephadex G-75 column. The kinetics data were Km = l.7 ${\times}10^{-3}M,\;-{\Delta}F^{\circ}$ = 3.99Kcal/mole, and $k^3=\;2.1{\times}10^{-2}\;sec^{-1}$. An analysis of the above data and other investigators' data obtained from some dipeptides led to the following conclusions. (1) Phenylalanyl residues in a synthetic peptide are bound to pepsin more strongly than glutamyl or tyrosyl residues, supporting the theory that a part of the binding region of the active center is hydrophobic. (2) Dipeptides are bound to pepsin principally through their side chains and the binding involves both side-chain residues. (3) The nature of amino acids in dipeptides $R_2-R_1,\;affect\;the\;k_3$ values.

• Applied Biological Chemistry
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• v.34 no.1
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• pp.1-7
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• 1991

Optimum conditions for hydrolysis of sunflower seed by pepsin and for plastein formation by pepsin were determined. The optimum conditions for hydrolysis of sunflower seed were pH 1.5, $45^{\circ}C$, enzyme concentration 2%, substrate concentration 2%, and hydrolysis time 24hr. The optimum conditions for sunflower seed-plastein formation were 50% substrate, pH 4.5, $50^{\circ}C$, 0.25% pepsin and 18hrs reaction time. To verify plastein fromation from concentrated prptic hydrolysate of sunflower seed, thin layer chromatography was performed. The TLC pattern of concentrated peptic hydrolysate of sunflower seed was different from that of its plastein. The TLC pattern of concentrated peptic bydrolysate of sunflower seed and at of its plastein indicated that plastein was different material from the hydrolysate.

• Korean Journal of Food Science and Technology
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• v.25 no.1
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• pp.39-45
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• 1993

The effects of enzymatic modification with pepsin and actinidin was studied on molecular weight distributions and functional properties of hydrolysates from soy protein isolate (SPI) differing in degree of hydrolysis. The hydrolyzed SPI by pepsin showed 41.5% degree of hydrolysis after 5 min, and maximum hydrolysis was obtained after 2 hours. Actinidin hydrolyzed SPI 26.71% degree after 1 hour. On SDS-PAGE, native SPI showed 9 distinguishable bands on SDS-PAGE gel. Pepsin treated SPI showed one broad band in the lower part of gel. This band was shifted further to the bottom of the gel and became faint as hydrolysis time increased. While actinidin treated SPI showed different SDS-PAGE pattern from pepsin. However PAGE patterns were similar with pepsin and actinidin treated groups. With pepsin treatment, solubility of SPI distinctively increased around isoelectric point(pI). Emulsifying activity (EA) and emulsifying stability (ES) showed marked increase over pH range of $3.0{\sim}8.0$. 5 min modified group had most excellent foam expansion (FE). Foam stability (FS) was increased as pepsin treatment time increased at pI. With actinidin treatment, solubility was increased. 60 min modified SPI had the most effective EA at pH 4.5. However ES was not effected by actinidin treatment. 5 min modified group was most effect in FE. FS was higher at alkaline pH.

• Journal of Dairy Science and Biotechnology
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• v.14 no.2
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• pp.135-146
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• 1996

This experiment was carried out to investigate the changes of casein of cheese base treated with substitute enzyme during ripening. The cheese base without enzyme treatment(control, D)and cheese base treated with only calf rennet(A), cheese base treated with mixed enzyme(calf rennet :porcine pepsin 1:1, B), cheese base treated with only porcine pepsin(C) were manufactured. The changes of casein were analyzed by means of HPLC and electrophoresis as experimental parameters during ripening. Gel filtration(HPLC) of casein by Superose 12 column in Cheddar cheese showed 5 fractions immediately after manufacturing and 8 fractions after six months ripening. Though D showed no difference in number of fraction(4 fraction) during 8 weeks ripening, A, B, C have represented the change of fraction number 4 to 5, 4 to 7, 4 to 8, respectively. As the mixing ratio of porcine pepsin increased, higher degradability of casein appeared. After 8 weeks ripening, electrophoresis of casein in cheese base showed three bands as an ${\alpha}$$_{s1}$casein from A and five bands from B, C. In case of D one major band and two minor bands were appeared as an ${\alpha}$$_{s1}$-casein. As the additional level of porcine pepsin increased the concentration of ${\beta}$-casein band decreased. however, that of ${\gamma}_1$ ${\gamma}_2$-casein band increased and para-${\kappa}$-casein band appeared from A, B, C, except D.