• Journal of the Korean Society of Food Science and Nutrition
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• v.17 no.3
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• pp.242-248
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• 1988

Plasteins were synthesized from a peptic sardine protein hydrolysate by pepsin, ${\alpha}-chymotrypsin$ pretense(from Aspergillus saitoi) and papain under the optimum conditions of previous paper. L -glutamic acid diethylester and L-leucine ethylester also were incorporated into plastein during the plastein reaction by papain. General composition, yield, molecular weight and amino acid composition were measured. The protein, ash and lipid rontent of plasteins were $81.1{\sim}88.2%$, $1.9{\sim}7.6%$ and $0.3{\sim}0.8%$, respectively. The yield of plasteins were pretense plastein 52.3%, papain plastein 44.2%, pepsin plnstein 43.6%, ${\alpha}-chymotrypsin$ plastein 43.2%. Leu -papain plastein 33. 2% and Glu - papain plastein 29.0%. The glutamic acid and leucine content in Glu -papain plastein and Leu -papain plastein were 39.0%, 37.5%, respectively. While the contents in the papain plastein were 14.3%, 7.1%, respectively. The amino acid composition of plasteins were similar to that of peptic sardine protein hydrolysate. The major molecular weight of the peptic hydrolysnte estimated by gelfilteration were 1,800 and 285, and those of plasteins were 26,000 and 9,100 for ${\alpha}-chymotrypsin$, 23,000, 10,000 and 4,300 for pepsin, 18,000 for pretense, 13,000 for papain, 29,000 for Leu -papain plastein and 19,000 for Glu -papain plastein.

• KSBB Journal
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• v.15 no.6
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• pp.664-669
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• 2000

Micellar aggregates are known to be useful for the selective isolation of biologically active materials such as amino acids, proteins, and enzymes from crude mixtures sparsely dispersed in water. In this study, the effects of pH, salt type and its concentration on the solubilization of $\alpha$-chymotrypsin into the organic micellar phase, which consisted of AOT (sodium 야(2-ethylhexy)sulfosuccinate) and iso-octane, were comprehensively examined. It was found that maximum extraction efficiency was attained at a pH below the isoelectric point of $\alpha$-chymotrypsin; at pH=5.0 for NaCl and KCl, and at pH=7.0 for $CaCl_2$and $MgCl_2$. In order to avoid complications stemming from the precipitationof protein at low pH interfaces, the protein concentrations in the organic and aqueous phases were directly measured. The size of the micelle water pool was estimated by measuring the molar ratio of the surfactant to the water, W(sub)o. The resulting values of W(sub)o were nearly constant at 30 and 19 for NaCl and KCl, respectively, and were independent of pH. The addition of 1:2 salts like $MgCl_2$and $CaCl_2$ led to much lower, but a constant value of, W(sub)o than the 1:1 salts.

• Korean Journal of Food Science and Technology
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• v.33 no.5
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• pp.603-610
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• 2001

The quality characteristics of soy yogurt prepared with different proteolytic enzymes and starter culture were evaluated. In order to facilitate the growth of lactic acid bacteria and subsequent production of lactic acid, soy protein isolate(SPI) was hydrolyzed using three kinds of proteases; one extracted from Aspergillus oryzae, bromelain and ${\alpha}-chymotrypsin$. The cultural systems employed thereafter for lactic fermentations were: 1) Bifidobacterium bifidum, 2) B. bifidum and Lactobacillus acidophilus, 3) B. bifidum and Lactobacillus bulgaricus. In soy yogurt, pH was more decreased by mixed culture method than single culture method with the accumulation of lactic acid. Viable cells of lactic acid bacteria in soy yogurts were measured $10^8$ CFU/g by the single culture method while $10^9$ CFU/g by the mixed culture method except ${\alpha}-chymotrypsin$ treatment. The amount of free amino acids in soy yogurts were substaintially increased by enzyme treatment. Viscosity was decreased by enzyme treatment, resulting in higher viscosity by ${\alpha}-chymotrypsin$ treatment. Water holding capacity was found to be higher in the single culture method in case of enzyme treatment. Among the various volatile flavor components isolated and identified after enzyme hydrolysis, acetaldehyde, ethanol, diacetyl, butyl alcohol contents tended to increase by lactic fermentation.

• Bulletin of the Korean Chemical Society
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• v.24 no.10
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• pp.1531-1534
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• 2003

• Applied Biological Chemistry
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• v.33 no.4
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• pp.287-292
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• 1990

Eight(I through VII) of Bowman-Birk proteinase inhibitor have been isolated from soybean with DEAE-Sephadex A-50. Inhibitor VII was a typical BBTI, showing high cysteine content(17%/mole) ud low trypsin to chymotrypsin inhibiting activity(TIA/CIA= 1.0) with the independent reactive site to each enzyme. Dissociation constant of trypsin-BBTI and chymotrypsin-BBTl complexes were $9.17{\times}10^{-9}M$ and $5.14{\times}10^{-8}M$, respectively. Inhibitor Vll was extremely heat stable. Six hours heat treatment at $100^{\circ}C$ caused only 50% decrease in it's original inhibiting activity. Except inhibitor III,6 other isoinhibitors differed from a typical BBTI in TIA/CIA, values, ranging from 3 to 29.

• 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.

• Food Science of Animal Resources
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• v.34 no.2
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• pp.151-157
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• 2014

This study investigated the effects of three proteases (trypsin, pepsin and chymotrypsin) on the hydrolysis efficiency of porcine placenta and the molecular weight (Mw) distributions of the placental hydrolysates. Because placenta was made up of insoluble collagen, the placenta was gelatinized by applying thermal treatment at $90^{\circ}C$ for 1 h and used as the sample. The placental hydrolyzing activities of the enzymes at varying concentrations and incubation times were determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and gel permeation chromatography (GPC). Based on the SDS-PAGE, the best placental hydrolysis efficiency was observed in trypsin treatments where all peptide bands disappeared after 1 h of incubation as compared to 6 h of chymotrypsin. Pepsin hardly hydrolyzed the placenta as compared to the other two enzymes. The Mw distribution revealed that the trypsin produced placental peptides with Mw of 106 and 500 Da. Peptides produced by chymotrypsin exhibited broad ranges of Mw distribution (1-20 kDa), while the pepsin treatment showed Mw greater than 7 kDa. For comparisons of pre-treatments, the subcritical water processing (37.5 MPa and $200^{\circ}C$) of raw placenta improved the efficiency of tryptic digestions to a greater level than that of a preheating treatment ($90^{\circ}C$ for 1 h). Consequently, subcritical water processing followed by enzymatic digestions has the potential of an advanced collagen hydrolysis technique.

• Applied Biological Chemistry
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• v.13 no.1
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• pp.81-85
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• 1970

In this studies, we isolated a kind of protein from Alisma Canaliculatum by the saline extraction. This protein was found to have a strong protective effects on the denaturation of ${\alpha}-chymotrypsin$ in the solution state. The obtained important results during the studies were as follows, 1. This protein was never hydrolyzed by the ${\alpha}-chymotrypsin$. 2. The denaturation of ${\alpha}-chymotrypsin$ was strongly protected by this sample protein. 3. Isoelectric point of this sample was about 4.7. 4. This sample protein was determined as an antigen but very weak antigenicity was indicated on rabbit.

• BMB Reports
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• v.44 no.6
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• pp.387-392
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• 2011

To investigate the molecular scavenging capabilities of the larvae of Hermetia illucens, two serine proteases (SPs) were cloned and characterized. Multiple sequence alignments and phylogenetic tree analysis of the deduced amino acid sequences of Hi-SP1 and Hi-SP2 were suggested that Hi-SP1 may be a chymotrypsin- and Hi-SP2 may be a trypsin-like protease. Hi-SP1 and Hi-SP2 3-D homology models revealed that a catalytic triad, three disulfide bonds, and a substrate-binding pocket were highly conserved, as would be expected of a SP. E. coli expressed Hi-SP1 and Hi-SP2 showed chymotrypsin or trypsin activities, respectively. Hi-SP2 mRNAs were consistently expressed during larval development. In contrast, the expression of Hi-SP1 mRNA fluctuated between feeding and molting stages and disappeared at the pupal stages. These expression pattern differences suggest that Hi-SP1 may be a larval specific chymotrypsin-like protease involved with food digestion, while Hi-SP2 may be a trypsin-like protease with diverse functions at different stages.

• Korean Journal of Food Science and Technology
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• v.22 no.4
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• pp.466-472
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• 1990

The effect of sugar addition and heat treatment on the myofibrillar protein extractability was studied. Maillard reaction was dependent on heating time significantly and glucose revealed the highest reactivity for Maillard reaction. The extractability of myofibrillar proteins was lowest in case of glucose addition and decreased according to increasing of heating time, Higher extractability was resulted in by digestion of myofibrillar proteins with enzymes after sugar addition and heat treatment than the undigested samples, as the sample was digested with trypsin that is the highest. And by digestion with trypsin, chymotrypsin and peptidase at a time the extractability of meat proteins increased remarkably.