• Korean Journal of Food Science and Technology
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• v.14 no.2
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• pp.106-111
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• 1982

To investigate the soybean trypsin inhibitors from seven varieties of soybeans and their twenty one $F_1-hybrids$, water soluble proteins were extracted. Trypsin inhibitors were isolated from those proteins and purified by sephadex G-75 column chromatography and polyacrylamide gel electrophresis. Total 16 kinds of trypsin inhibitors were isolated. From each variety of soybeans, $5{\sim}12$ kinds of trysin inhibitors could be detected and among them, 5 kinds of trypsin inhibitors were mainly distributed.

• Korean Journal of Microbiology
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• v.40 no.2
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• pp.178-182
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• 2004

In the vegetative hyphae of Aspergillus nidulans, a zymogenic form of the class I chitin synthase activity was successfully measured by the assay condition for Saccharomyces cerevisiae class I chitin synthase, Chsl. The class I chitin synthase activity of the A. nidulans chsC wild type strain was increased about six-fold by trypsin-pretreatment, but that of the chsC disruption strain revealed no increase. Interestingly enough, level of the class I chitin synthase activity of the chsC disruption strain was almost the same as that of the chsC wild type without trypsin-pretreatment. These results indicated that the A. nidulans ChsC activity could be measured by account-ing the class I chitin synthase activity without the trypsin-pretreatment as an internal control. Consistence to the expression pattern of the chsC revealed by northern blot analysis, the activity of ChsC was increased upon reaching the culture time for acquiring developmental competence. Our results shown here also supported the previous report suggesting the possible involvement of ChsC in vegetative hyphal growth of A. nidulans.

• Korean Journal of Food Science and Technology
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• v.28 no.1
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• pp.99-104
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• 1996

Carbohydrate-free caseinomacropeptide (CMP) was isolated from the sweet whey powder by a precipitation method using 12% trichloroacetic acid. The yield of carbohydrate-free CMP was 2.7 g from 100 g sweet whey powder. The electrophoretic pattern and the amino acid analysis of CMP showed that isolated CMP was quite pure, indicating the precipitation with 12% trichloroacetic acid was very effective for isolating carbohydrate-free CMP from the sweet whey powder. Trypsin, covalently immobilized on pore glass beads by carbodiimide (EDC) method, was 20mg per 1g glass beads. CMP was almost completely hydrolyzed by soluble trypsin in 24hr, but not by immobilized trypsin. The tryptic hydrolysates were fractionated on a Bio-Gel P 4 column $(1.5{\times}120\;cm)$and separated peptides were tested for their capacities to inhibit platelet aggregation using a aggregometer. The hydrolysate obtained from CMP after 24hr digestion by immobilized trypsin showed the highest activity.

• Journal of Chest Surgery
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• v.43 no.6
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• pp.565-575
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• 2010

Background: Various decellularization methods have been studied in order to develop tissue graft which is less immunogenic and more durable. This study was performed to investigate the physico-dynamic and histological effect of trypsin pretreatment on decellularization protocols. Material and Method: Two groups of bovine pericardium specimen each underwent decellularization process based on SDS and Triton X-100 or N-lauroylsarcosinate and Triton X-100. Two more groups additionally underwent pretreatment with 0.1% Trypsin/0.1% EDTA. After decellularization process, mechanical tensile strength was tested, then biomechanical test of permeability and compliance was tested before and after fatigue test. Light microscopy and electron microscopy was performed to observe histological findings. Result: There was no difference in mechanical tensile strength between groups, but permeability and compliance was decreased in trypsin pretreated groups. Light microscopic and electron microscopic findings revealed damage of the extracellular matrix in trypsin pretreated groups and in groups which underwent the fatigue test also. Conclusion: Trypsin pretreatment in decellularizing process of bovine pericardium damages extracellular matrix and increases permeability and compliance of the bovine pericardium, but did not decrease tensile strength. Further studies are needed to use enzymatic treatments in decellularization protocols.

• KSBB Journal
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• v.4 no.2
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• pp.123-127
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• 1989

The separation of trypsin inhibitir using reverse micellar system was invertigated. Among the biffer system tested, 1.0M $CaCl_2$ solution (pH 3.0) and 1.0M NaCl soluation (pH 11.5) were most effective for solubilization and de-solubilization of protein, respectively. When these conditions were applied to two model sampeles, one of which was composed of the same amount of 7S protein and trpsin inhibitor, and the other of which was composed of the same amount of soluble soybean protein isolates and trypsin inhibitor, highly pure trypsin inhibitor was obtained. And in the real soybean, Kwng Gyo, pure trypsin inhibior was also obtained.

• Applied Chemistry for Engineering
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• v.5 no.2
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• pp.321-326
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• 1994

The water-soluble polyphosphazene possessing ether side groups was exposed to ${\gamma}-rays$ to prepare hydrogens with good water-swellability. The physical strength of these hydrogels could be controlled by irradiation dose of ${\gamma}-rays$. Trypsin and water-soluble polyphosphazene were irradiated together by ${\gamma}-rays$ for entrapment of enzymes into hydrogel networks. The activities of immobilized trypsin were examined spectrophotometrically after the reaction with N-${\alpha}$-benzoyl-1-arginine-p-nitroanilide in phosphate buffer. The immobilized trypsin was found to have good activity yield and suability after at least 500 hours.

• Journal of the Korean Chemical Society
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• v.34 no.3
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• pp.288-296
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• 1990

Antielastic fragment in GBⅠ-Ⅱ differ on $P_1$ site with that of antitryptic fragment in LBI. To obtain further understanding of the role of amino acid residue near the reactive site, specificity of $P_1$ site and loop size, Tyr substituted cyclic nonapeptide and cyclic pentapeptide were synthesized and the inhibition constants for some proteinases were calculated by Dixon method. Cyclic nonapeptide showed no inhibition for chymotrypsin but appeared low inhibitory activity for trypsin and elastase and that of cyclic pentapeptide possessed inhibitory activity for chymotrypsin.

• Applied Chemistry for Engineering
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• v.5 no.2
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• pp.305-312
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• 1994

The fed-batch process which combinded high selectivity of affinity chromatography and membrane process was developed. The mixture of trypsin and chymotrypsin, having almost the same molecular weight and the chemical structure, were used as model enzymes. The water soluble polymer having more affinity for trypsin and celluose acetate membrane gelated in 50vol.% ethanol for removing free enzymes and retentating trypsin-affinity polymer complex simutaneously were used in this system. The membrane pore size was controlled by ethanol concentration in the gellation bath, and the affinity polymer was prepared by polymerization of acrylamide with N-acryloyl-m-aminobenzamidine at $4^{\circ}C$. The trypsin could be effectively concentrated by utilizing an affinity polymer and a prepared UF-50 ultrafiltration membrane. As a result, 86% purity trypsin was recovered by the current purification process.

• Microbiology and Biotechnology Letters
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• v.36 no.1
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• pp.28-33
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• 2008

The expression vector (pWHM3-TR1R2) for sprT gene encoding Streptomyces griseus trypsin (SGT) followed by two regulatory genes, sgtR1 and sgtR2, was introduced into Streptomyces lividans TK24 and Streptomyces griseus IFO 13350. Various media with different compositions were used to maximize the productivity of SGT in the recombinant trains. he SGT productivity was best when the transformant of S. lividans TK24 was cultivated in R2YE medium (0.74 unit/mL) at 5 days of cultivation. C5/L (0.66 unit/mL) medium also gave a good productivity, but Livid (0.08 unit/mL) and NDSK (0.06 unit/mL) yielded poor productivities. S. griseus IFO 13350/pWHM3-TR1R2 produced SGT by 1.518 unit/mL (C5/L), 1.284unit/mL (R2YE),0.932 unit/mL (NDSK), and 0.295 unit/mL (Livid) at 7 days of cultivation, which was much higher than those from S. lividans TK24/TR1R2. The SGT protein was purified from the culture broth of S. griseus IFO 13350/pWHM3-TR1R2 in C5/L to homogeneity via ammonium sulfate fractionation, and CM-sepharose and SP-sepharose column chromatographies. The specific activity of purified SGT was 69,252 unit/mg, and the final purification fold and recovery yield were 6.5 and 1.4%, respectively.

• Korean journal of food and cookery science
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• v.13 no.2
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• pp.168-172
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• 1997

Yolk immunoglobulins (yIgG) from hen's egg were purified. To investigate the stability of yIgG to digestive enzymes, the changes of antigen binding activities (ABC) after in vitro proteolysis were examined by competitive ELISA. After 30 min exposure to pepsin, the ABC of yIgG was lost. However, comparing with native yIgG, the ABC of pepsin digested yIgG was decreased, but considerable amount of ABC was remained after 30 min exposure to pepsin in 50% saccharose solution. Therefore, the stability of yIgG to pepsin digestion was improved by the addition of saccharose to yIgG solution. The ABC of yIgG was considerably remained after exposure to trypsin and chymotrypsin for 8 hr. YIgG showed especially good stability to chymotrypsin proteolysis.