• Journal of the Korean Society of Food Science and Nutrition
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• v.27 no.6
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• pp.1117-1124
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• 1998

Chymosin was purified from commercial rennet with DEAE Sepharose CL 6B and immobilized on CeliteTM using glutaraldehyde. Whole casein from fresh raw milk was hydrolyzed by immobilized chymosin and total CMP was isolated by trichloroacetic acid(TCA) and ultrafiltration, and characterized. The amount of chymosin purified from 15g commercial rennet by DEAE Sepharose CL 6B was 0.16g and 18mg of chymosin was immobilized on 1g of CeliteTM by 5% glutaraldehyde. Immobilized chy mosin hydrolyzed most of casein on whole casein within 2 hours to leave para casein and casei nomacropeptide(CMP). The total CMP isolated from 10g of whole casein hydrolyzate by TCA and ultrafiltration was 0.4g and 0.1g, respectively. Results of electrophoresis, amount of sialic acid, com position of amino acid and ratio of A280 to A214 showed that total CMP by TCA was purer and had more CMP without carbohydrate than one by ultrafiltration. CMP isolated from total CMP by 12% TCA precipitation was 50% of total CMP and most of caseinoglycopeptide(CGP) was removed from total CMP, indicating less amount of sialic acid in CMP than in total CMP.

• Applied Biological Chemistry
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• v.38 no.3
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• pp.254-258
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• 1995

Various artificial casein micelle systems were prepared from dephosphorylated whole casein, ${\beta}$- or ${\kappa}$-casein and their stabilities towards ethanol were assessed. Ethanol stability was lower in the micelle systems with dephesphorylated whole casein as compared to the artificial micelles prepared from native whole casein, and the stability decreased with the extent of dephosphorylation. The casein micelles with partially dephosphorylated ${\kappa}$-casein had a lower ethanol stability than those with native ${\kappa}$-casein. Ethanol stability of the micelle system with dephosphorylated ${\beta}$-casein decreased as the degree of dephosphorylation increased. Progressive dephosphorylation of caseins in skim milk system resulted in a decrease of the stability towards ethanol. The decrease was less than that in the system with dephosphorylated individual caseins. Increase in pH of the artificial casein micelle systems in the range of $6.3{\sim}7.2$ led to an increased ethanol stability manifesting that the presence of serine phosphates contributes significantly to the stability towards ethanol.

• Korean Journal of Agricultural Science
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• v.36 no.1
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• pp.111-122
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• 2009

When the cattail pollen was identified by using fibrinolytic agents, we found that the fibrinolytic activity was controlled by an enzyme. Therefore, for determining the fibrinolytic activity of cattail pollen, the fibrinolytic enzyme in cattail pollen was purified by gel filtration using DEAE-cellulose, Sephadex G-150 and HPLC. Also, its purity was certified by polyacrylamide gel electrophoresis, and its physico-chemical properties, such as pH and temperature stabilities and effects of metal, inhibitors and substrates, were examined. The specific activity, purification fold, and molecular weight of the enzyme were 38U/mg, 86.4,and 75kDa, respectively. The optimum pH for the purified enzyme was at 4.0 and it was stable at pH 4.0-6.0. The optimum temperature was $55^{\circ}C$ and it was stable at $30-60^{\circ}C$. But the enzyme began to be inactivated at $70^{\circ}C$ and its activity was totally lost at temperatures above $80^{\circ}C$. As for substrate specificity, the enzyme was most effective in dissolving fibrin, followed by whole casein, ${\kappa}$-casein, ${\alpha}$-casein, ${\beta}$-casein, and BSA. With casein as the substrate, Km value was found to be 0.44mM and the enzyme showed a high affinity for casein. As for the metal ions affecting enzyme activity, $K^+$, $Na^+$, and $Mg^{2+}$ had no effect on enzyme reaction while $Zn^{2+}$ and $Fe^{2+}$ showed potent inhibitory activity. Judging from the fact that the purified enzyme was also strongly inhibited by PMSF, iodoacetic acid, and SDA, it assumed to be a serine protease.

• Food Science of Animal Resources
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• v.37 no.6
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• pp.940-947
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• 2017

Goat milk has a protein composition similar to that of breast milk and contains abundant nutrients, but its use in functional foods is rather limited in comparison to milk from other sources. The aim of this study was to prepare a goat A2 ${\beta}$-casein fraction with improved digestibility and hypoallergenic properties. We investigated the optimal conditions for the separation of A2 ${\beta}$-casein fraction from goat milk by pH adjustment to pH 4.4 and treating the casein suspension with calcium chloride (0.05 M for 1 h at $25^{\circ}C$). Selective reduction of ${\beta}$- lactoglobulin and ${\alpha}_s$-casein was confirmed using sodium dodecyl sulphate-polyacrylamide gel electrophoresis and reverse-phase high-performance liquid chromatography. The hypoallergenic property of A2 ${\beta}$-casein fraction was examined by measuring the release of histamine and tumor necrosis factor alpha from HMC-1 human mast cells exposed to different proteins, including A2 ${\beta}$-casein fraction. There was no significant difference in levels of both indicators between A2 ${\beta}$-casein treatment and the control (no protein treatment). The A2 ${\beta}$-casein fraction is abundant in essential amino acids, especially, branched-chain amino acids (leucine, valine, and isoleucine). The physicochemical properties of A2 ${\beta}$-casein fraction, including protein solubility and viscosity, are similar to those of bovine whole casein which is widely used as a protein source in various foods. Therefore, the goat A2 ${\beta}$-casein fraction may be useful as a food material with good digestibility and hypoallergenic properties for infants, the elderly, and people with metabolic disorders.

• Journal of Nutrition and Health
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• v.16 no.2
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• pp.81-88
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• 1983

This study was performed to investigate the influence of the amino acid composition of diet and environment on RNA, protein content in brain and learning ability in rats. Forty-two Sprague-Dawley male rats were divided into six groups according to type of diet, casein, soybean meal, or corn gluten and rearing condition, isolated or enriched. They were fed foods ad libitum for 6 weeks. A water maze was used to test behavioral performance for 3 weeks from 4th week. The rats were sacrificed at 6th week and their whole brains were taken and frozen for assay of RNA and protein. The results were summarized as follows : 1) The body weight gain for the experimental periods of corn gluten group was significantly lower than the casein and the soybean meal group. 2) The brain weight of the corn gluten group was significantly lower than the casein and the soybean meal group and the environmental enrichment slightly increased it among rats fed the corn gluten diet. 3) The total RNA contents were the greatest in the environmentally enriched casein group. The brain protein contents of the isolated corngluten group was the smallest. However, the contents of the enriched corn gluten group were similar to those of the others. 4) In the water maze test, the isolated corngluten group spent significantly more time than the others. Environmental enrichment could decrease time to perform the task of the maze.

• Journal of Nutrition and Health
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• v.17 no.1
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• pp.20-30
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• 1984

This experiment was designed to investigate the effects of the mixing ratio of soyprotein and casein, and the level of pectin combined with the mixture on lipid metabolism in rats. Forty-eight male weanling rats of Wistar strain weighing 58.8\;{\pm}\;1.9g$ were divided into six groups by completely randomized block design and fed 10% protein diet for four weeks. Two types of protein mixtures (casein to soyprotein mixing ratio of 1 : 3 and 2: 1)combined with 0.5% , 3%, and 5% of pectin were employed for experimental diets. The results obtained in the study are summarized as follows ; 1) Feed efficiency ratio and protein efficiency ratio were not significantly different among six groups for the whole experimental period, but those for high casein-low pectin group were significantly higher than the ones for high soy-high pectin group at 4th week of the experimental period. 2) Gross fecal dried weight and fecal lipid excretion were higher in high pectin groups of both protein combinations. Therefore, the apparent fat digestibility and absorption appeared to be significantly low in high pectin groups. 3) Pectin was effective in lowering serum lipid and cholesterol levels in high casein groups, but no effect of pectin was noted in high soyprotein groups. 4) Lipid and cholesterol contents of the liver were higher in high soy-low pectin group than the others. And no marked differences in lipid and cholesterol contents in the kidney and carcass were observed.

• Journal of Dairy Science and Biotechnology
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• v.40 no.4
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• pp.173-181
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• 2022

Industrial-scale Ca-fortified Dangmyon was manufactured with added casein phosphopeptides (CPP) to increase Ca adsorption in the intestine. Very low P content in eggshell Ca (egg Ca) and Dangmyon could make it possible to indirectly measure CPP content in Dangmyon. Partitions of the whole P present in Dangmyon were made into sweet potato, egg Ca, and CPP. The CPP content was obtained by multiplying CPP per P by the amount of P partitioned into CPP. It was found that 88.46% of CPP was obtained. However, when milk Ca, which was much higher in P, was added to fortify Dangmyon with CPP, it was found that the CPP content was either under- or over-estimated. Care must be taken when a much higher content of P as a Ca source is selected using this method. It was discovered that the added Ca and CPP were retained after cooking at boiling temperature; therefore, Dangmyon could be an excellent Ca and CPP carrier for humans.

• Korean Journal of Food Science and Technology
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• v.32 no.3
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• pp.564-569
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• 2000

An enzyme-linked immunosorbent assay(ELISA) was developed for the detection of milk proteins in processed foods. The ${\alpha}_{s1}-casein({\alpha}_{s1}-CN)$, a heat stable major milk protein, was immunized into rabbits to produce specific antibodies. When competitive indirect ELISA(ciELISA) using $anti-{\alpha}_{s1}-CN$ antibodies was established, its detection limit was $0.1\;{\mu}g/mL$. The reactivities of the specific antibodies toward ${\alpha}_{s1}-CN$, skim milk, ${\beta}-CN$ and whey protein isolate(WPI) were 100, 37, 0.14 and 0.04%, respectively, as determined by ciELISA. However $anti-{\alpha}_{s1}-CN$ antibodies did not have any reactivity to other milk proteins such as ${\beta}-lactoglobulin,\;{\alpha}-lactalbumin$, bovine serum albumin, and isolated soy protein. When sandwich ELISA was established, its detection limit was $0.01\;{\mu}g/mL$ which was 10 times more sensitive than that of ciELISA. In the spike test which was performed by adding 1-10% of whole CN to market milk, mean assay recovery as determined by sandwich ELISA was 94.8%(CV, 8.2%). Food stuffs and dairy products were assayed by sandwich ELISA to show 29, 0.13, 0.25, and 6.9% of whole CN in skim milk powder, WPI, semi-solid yoghurt, and processed cheese, respectively.

• KSBB Journal
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• v.9 no.1
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• pp.72-84
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• 1994

A model to explain the observed kinetics in a whole process of Cheddar-cheese ripening has been developed. It includes growth and lysis of cells in the cheese matrix, cell-wall bound protelnases and intracellular dipeptidases that are released into cheese upon cell lysis, and the production of dipeptides and amino acids from casein in cheese. Model simulations have been conducted to figure out the crucial factors in the process of the cheese ripening. The influential factors have been found to be the cell numbers and the dipeptidase activity at the beginning of the cheese ripening, and the cell-lysis rate of cheese starters. The simulation results have also suggested the use of a mixed culture as well as the experimental screening for a more suitable organism as a cheese starter hence, the model shows how to accelerate the cheese ripening.

• 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.