• Journal of the East Asian Society of Dietary Life
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• v.19 no.1
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• pp.45-51
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• 2009

In this study, food protein hydrolysates were prepared from six types of food protein: purified meat protein, whole egg protein, casein, isolated soy protein, concentrated rice protein, and gluten. Food proteins were hydrolyzed with pepsin and ethanol (80%)-soluble fractions of pepsin hydrolysates were employed for analysis. The products were colorless and odorless powders with low fat content and good solubility. The MW (molecular weight) of the protein hydrolysates was confirmed to be $200{\sim}1,800$ via gel filtration. Free amino acid contents accounted for less than 5% of the samples. The results of our amino acid analysis revealed that all food protein hydrolysates preserved their original amino acid compositions and nutritional values of their source proteins with highly pure oligopeptide mixtures. These results show that the food protein hydrolysates prepared in these investigations should prove excellent dietary nitrogen sources for a variety of applications.

• Korean Journal of Food Science and Technology
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• v.27 no.3
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• pp.329-335
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• 1995

Rheological properties of whole soybean gel(soygel) were investigated as affected by the water addition ratio, stirring time and Ca salts. The soygel was prepared by suspension of whole soy flour(WSF, 300 mesh) in boiling water, addition of sodium alginate and Ca salts followed by thorough mixing and gel formation at $4^{\circ}C$. The texture properties of hardness, adhesiveness and cohesiveness of the gel were increased as the stirring time prolonged from 5 to 30 minutes. From the results of the rheological and sensory properties, 20 minutes of stirring time was selected for whole soybean gel preparation. Eventhough increase in water addition ratio from 8 to 12 times(water/WSF, v/w) resulted a decrease in hardness and adhesiveness, 10 times ratio was chosen as proper the water addition based on textural uniformity. Among the Ca salts, $CaSO_4$ produced the highest hardness followed by Ca $gluconate-CaSO_4$ mixture(413g) and Ca gluconate at the water addition level of 10 times. In order to determine the amounts of Ca salts, and 0.125g of Ca gluconate or $CaSO_4$ per g WSF were found to be optimum in terms of textural and sensory properties. The proper mixing ratio of Ca gluconate and $CaSO_4$ was found to be 50 : 50, 25 : 75 and 0 : 100.

• Applied Biological Chemistry
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• v.40 no.3
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• pp.178-183
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• 1997

A protease was purified from Bacillus subtilis CCKS-111 by ammonium sulfate treatment, DEAE-cellulose ion-exchange chromatography, Sephadex G-100 gel filtration and high performance liquid chromatography (HPLC). The specific activity of the purified enzyme was 24.3 unit/mg protein and the purification fold of enzyme was 50.6. Molecular weight of the purified enzyme estimated about 28,000 by HPLC gel filtration. The amino acid residues of this enzyme were 251.3 except threonine, serine and glycine. This result was similar to Bacillus subtilis subtilisin DY. From the first N-terminal amino acid to the 32th amino acid, the amino acid sequence was estimated after RP-HPLC elution. N-terminal and the 32th amino acids were alanine and aspartic acid. Alanine, serine, glycine and arginine were four major acids in the enzyme.

• Journal of Life Science
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• v.22 no.6
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• pp.823-827
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• 2012

A bacterial strain producing a fibrinolytic enzyme, subtilisin CP-1, was isolated from Doen-Jang, a Korean traditional fermentation food. Based on the analysis of gene sequence of 16S rRNA and biochemical analysis, the strain was identified as Bacillus sp. and named as Bacillus sp. CP-1. To investigate the effect of the medium on the production of fibrinolytic enzyme from Bacillus sp. CP-1, two commercial bacterial culture media, tryptic soy broth (TSB) and Luria-Bertani (LB), were applied to the cultivation of Bacillus sp. CP-1. The strain secreted only one proteolytic enzyme (subtilisin CP-1) in the culture broth. The molecular weight of subtilisin CP-1 was estimated to be 28 kDa. Subtilisin CP-1 was optimally active at pH 9.0 and $45^{\circ}C$, and exhibited high specificity for Meo-Suc-Arg-Pro-Tyr-pNA (S-2586), a synthetic chromogenic substrate for chymotrypsin. The first eight amino acid residues of the N-terminal sequence of the enzyme are AQSVPYGI; this sequence is identical to that of subtilisin NAT and E.

• Journal of the Korean Society of Food Science and Nutrition
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• v.46 no.8
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• pp.965-970
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• 2017

The objective of this study was to evaluate the effects of gelatin type (powder vs. hydrated) with or without transglutaminase (TGase) on the physicochemical and textural properties of low-fat model sausages (LFS). Treatments included LFS (control), LFS with hydrated-gel form of gelatin (1%), and LFS with powder form of gelatin (1%). Yellowness values of LFS with any type of gelatin were higher than those without gelatin (P<0.05). Moisture content (%) of LFS containing powder form of gelatin (1%) was higher than those with hydrated-gel form of gelatin or control (P<0.05). Expressible moisture (EM, %) of LFS with hydrated-gel form of gelatin was lower than those with powder form of gelatin (P<0.05). Thus, sausages with hydrated-gel form of gelatin showed better functional properties as compared to those with powder form of gelatin. To elucidate the interaction between gelatin and TGase in meat product, five actual sausages were manufactured: reference [konjac flour (KF), carrageenan (CN), and soy protein isolate], control (KF and CN alone), TRT1 (KF and CN, TGase 1%), TRT2 (KF and CN, gelatin 1%), and TRT3 (KF and CN, TGase 1%+gelatin 1%). EM (%) of sausages with TGase alone was higher than those of other treatments (P<0.05). Most textural properties of TRT3 were higher than those of other treatments. Thus, TRT3 showed better functional properties than those with single addition. In conclusion, a combination of TGase and gelatin could be used to manufacture LFSs with improved functional and textural properties.

• Applied Biological Chemistry
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• v.31 no.4
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• pp.361-370
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• 1988

To investigate the interaction between whey and soybean protein, thermal changes of component proteins were analyzed by column chromatography and gel electrophoresis. In the Sephadex G-200 chromatography of the mixture treated at above $80^{\circ}C$, the amount of low molecular weight proteins and high molecular aggregates were increased. This implicated that dissociation of 1ls globulin into subunits and the formation of soluble aggregates between these subunits and whey proteins that contain thiol and disulfide groups. These interaction between soy proteins and ${\beta}-lactoglobulin$, ${\alpha}-lactalbumin$, and proteose-peptone 3 were confirmed by gel electrophoresis. Bovine serum albumin, Immunoglobulin-G(H), Lactoferrin, 1ls-subunits(basic and acidic), and subunit of 7s globulin were also considered to interact each other depending on the condition of the salt solutions.

• Korean Journal of Food Science and Technology
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• v.32 no.6
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• pp.1379-1388
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• 2000

Ethanol extracts from Ruta graveolens Linne exhibited strong antimicrobial activities by disc diffusion method against 5 strains of Listeria monocytogenes (ATCC 19111, ATCC 19112, ATCC 19113, ATCC 19114 and ATCC 15313). Ethanol extract from Ruta graveolens Linne was subsequently fractionated by n-hexane, chloroform, ethyl acetate and water. Chloroform fraction of Ruta graveolens Linne showed strong growth inhibition at concentrations as low as 40 ppm level in broth culture medium against 5 strains of L. monocytogenes for 72 hr at $30^{\circ}C$. Single substance(RTG1-1) was isolated by silica gel column chromatography from chloroform fraction of Ruta graveolens Linne. RTG1-1 showed a strong bactericidal activity against L. monocytogenes at a concentration of 20 ppm level. Purified RTG1-1 was identified as gravacridonechlorine by analyses of EI-Mass, $^1H-NMR$ and $^{13}C-NMR$.

• Journal of the Korean Society of Food Science and Nutrition
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• v.29 no.5
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• pp.843-848
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• 2000

The single cell-gel electrophoresis assay (comet assay) was used to identify irradiated beans. Soy beans, kidney beans, and red beans were irradiated with $^{60}Co$ gamma rays at 0.1, 0.3, 0.5, 0.7, and 1.0 kGy. Beans were peeled out, crushed lightly, and treated with phosphate-buffered saline (PBS) to extract cells. The extracted cell suspension was mixed with agarose gel solution and spread on an agarose precoated slide. After lysis of the cells, they were subjected to microgel electrophoresis for 2 minutes, and then silver-stained. We found that the DNA fragments of the irradiated samples were stretched, migrated out of the cells, and formed tails towards the anode giving the appearance of comets, while the unirradiated or the undamaged cells formed very short or no tails. The tail lengths of irradiated samples were significantly increased as irradiation dose increased at the above 0.3 kGy.

• Preventive Nutrition and Food Science
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• v.8 no.3
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• pp.278-283
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• 2003

Textural properties of tofu manufactured with micronized full-fat soyflour (MFS) were enhanced by the addition of soy protein isolate, whey protein concentrate, chitosan oligosaccharide and mushroom powder. The MFS solution (14.2% solid content) was converted to semi-solid tofu by a two-stage heat treatment with the addition of 4% coagulant mix. The MFS tofu was evaluated by a compression test as well as sensory evaluation. To produce the semi-solid gel (MFS tofu) with reasonably high strength and toughness, the MFS solution with 14.2% solid content and 7.0% protein had to be heat treated at 121$^{\circ}C$ for 3min. The relative toughness of MFS tofu was increased by the addition of SPI, showing a 144% increase. The toughness of MFS tofu prepared with the MFS/SPI mixture was greatly increased by the addition of WPC at the level of 0.7% and the water separation from MFS tofu was greatly reduced. Furthermore, the toughness and strength of MFS/SPI tofu was enhanced by the addition of 0.1% chitosan oligosaccharide and 0.2% mushroom powder. The sensory evaluation of the tofu fortified with SPI, chitosan oligosaccharide and mushroom powder was superior to that of MFS tofu, with a higher score for overall preference.

• Journal of Dairy Science and Biotechnology
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• v.16 no.2
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• pp.98-105
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• 1998

Various peptides derived from food are among the most potent physiologically active agents known, and include anticancer peptides, angiotensin converting enzyme(ACE) inhibitor exhibiting antihypertension action, opioid peptides, antithrombotic peptides, hypocholesterolemic peptides, immunomodulators, calcium absorption enhancers, and other peptides. Hydrophobic peptides extracted from a Cheddar-type cheese slurry were fractionated by gel chromatography and repeated HPLC. A peptide fraction from HPLC showed high cytotoxicity on the tumor cell lines such as a human colon carcinoma, and comprised of Tyr, Ser, Leu, Gly, and others. Hypocholesterolemic peptides were isolated from peptic hydrolyzates of casein and soy proteins. Macropeptides of 1,000${\sim}$5,000 dalton were effective on reducing the cholesterol level of mouse serum. Peptides showing high Krigbaum hydrophobicity and ANS surface hydrophobicity resulted in high hypocholesterolemic effect and fecal steroid concentrations. Caseinomacropeptides(CMP) were isolated from whey powder and treated with soluble and immobilized trypsin to obtain antithrombotic peptides. One fraction from the CMP hydrolyzed with immobilized trypsin for 24h exhibited high antithrombotic activity with 52.5% inhibition of platelet aggregation. These result suggested that peptides from various milk products could be utilized as a good bioactive agents for developing health functional foods.