• 한국식품과학회지
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• 제20권2호
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• pp.170-175
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• 1988

초유 casein micelle의 특성을 조사하였다. 분만직후의 초유로부터 정상유로 이행됨에 따라서 총단백질의 함량은 감소하였으며, casein과 유청단백질의 비율에 있어서 casein은 증가한 반면 유청단백질은 감소하였다. 한편 탈지시킨 초유를 $100,000{\times}g$에서 10분(pellet 1), 30분(pellet 2)및 60분(pellet 3)동안 초원심분리하여 casein micelle을 크기별로 분리하였고, 상징액 중의 casein(serum casein)을 pH4.6에서 산침전 시킴으로 제조하였다. 분만직후의 초유로부터 정상유로 시간이경과함에 따라서 크기가 큰 micelle (pellet 1)의 양은 점차 감소하는 경향을 나타내었고, 중간크기의 micelle (pellet 2)의 양은 분반직후의 것을 제외하면 거의 일정한 수준을 유지하였으며, 작은 크기의 micelle (pellet 3)의 양은 점차 증가하였고, serum casein의 양은거의 일정하게 나타났다. 또 초원심분리에 의하여 얻은 각 casein micelle의 casein함량 중 ${\alpha}_{s1}-$및${\alpha}_{s2}-casein$과${\beta}-casein-5P$의 양은 micelle의 크기가 작아짐에 따라 감소하였으나, x-casein의 양은 현저히 증가하였으며, ${\beta}-casein-1P$(f29~209), (f106-209) 및 (f108~209)의 양에 있어서는 큰 차이가 없었다. 또 serum casein의 조성은 전 casein과 비교하여 볼 때 차이가 있었다.

• Journal of Nutrition and Health
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• 제27권7호
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• pp.699-708
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• 1994

This study aimed to verify the nutritional and curative effects of protein hydrolysate in rats with cysteamine-induced duodenal uncer. Duodenal ulcer rat model was established by intraperitoneal injections of cysteamine. Sprague-Dawley, female rats weighing approximately 200g were intraperitoneally injected twice cysteamine(13mg/100g BW) at intervals of 3h per day. This procedure was repeated 3$\times$at intervals of 3d. Animals fed on 10% casein diet for infection periods. After last injection, 4 kinds of diets(10% casein, 20% casein, 10% casein hydrolysate, 20% casein hydrolysate) were given. Gastric montility, trypsin activity in gastrointestinal content, retention rate of nitrogen, plasma total protein, albumin, amino-N, urinary urea nitrogen, creatinine and hydroxyproline were analyzed for nutritional effects of dietary nitrogen levels(10%, 20%) and sources(casein, casein hydrolysate). In duodenal ulcer rat model, there was no differences between 20% casein diet and 20% casein hydrolysate in the view of severeness of ulcer, gastric emptying rate, serum total protein, serum albumin, plasma $\alpha$-amino-N, UUN, creatinine excretion, GFR, nitrogen retention. On the other hand, rats on 10% casein hydrolysate diet group had more curative effect of the ulcer, higher plasma albumin concentration and nitrogen retention than 10% casein diet group. The casein hydrolysate diet group was lower trypsin activity in small intestinal content than the casein diet group, at both nitrogen levels(10%, 20%). The results suggest that protein hydrolysate be applied in diet therapy for the patients with gastrointestinal ulcer.

• Journal of Nutrition and Health
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• 제28권4호
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• pp.291-297
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• 1995

This study aimed to verify the nutritional and curative effects of protein hydroysate in rats model with gastric ulcer induced by restraint and water-immersion stress. Sprague-Dawley, famale rats weighing approximtely 200g were forced in 5$\times$5$\times$15cm plexiglas cage. The restraint and water immersion stress was carried at 20$\pm$2$^{\circ}C$ for 8-hours. After stress 4 kinds of diets(10% casein, 20% casein, 10% casein hydrolysate, 20% casein hydrolysate) were given for 5 days. In the gastric ulcer rats model, the growth, gastric emptying rate, trypsin activity in gastrointestinal content, plasma total protein, albumin, $\alpha$-amino-N, UUN, creatinine and hydroxyproline of the urine and nitrogen retention were analyzed for nutritional effects of dietary nitrogen levels(10%, 20%) and sources (casein, casein hydrolysate). The results were as follows ; In gastric ulcer rats model, severeness of ulcer, plasma protein, gastric emptying rate, nitrogen retention rate were not different between 20% casein-fed group and 20% casein hydrolysatefed group. But 10% casein hydrolysate-fed group had more curative group. The casein hydrolysate diet-fed group was lower trysin activity in small intestianl content than the casein-fed group, at both casein level(10%, 20%). Finally at 20% levels, there was no difference between casein and casein hydrolysate diet, but 10% level, casein hydrolysate diet was more curative of ulcer than casein diet in gastric ulcer rat model. The results of this study provide useful information concerning diet therapy for the patients with gastrointestinal diseases and the field of enteral diet materials.

• Applied Biological Chemistry
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• 제35권6호
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• pp.479-484
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• 1992

Cheddar 치즈의 숙성기간을 단축시키고 flavor를 증진시킬 목적으로 단백분해력이 있는 Micrococcus sp. LL3를 Cheddar 치즈에 첨가하기 위하여 본 균의 균체생산을 위한 최적배양 온도와 pH 및 배양시간에 따른 casein의 분해형태를 관찰하였다. 본 균주의 생육을 위한 최적 배양온도는 $30^{\circ}C$, 단백분해 효과의 최적 배양온도는 $37^{\circ}C$이었으며, 초기 배양 pH 7.0에서 균의 생육과 단백분해 효과가 가장 좋았다. 배양기간 중 정지기 초기의 세포에서 aminopeptidase의 효소활성이 가장 높았으며, 본 효소의 열 안정성이 높아 $50^{\circ}C$에서 20분간 열처리 후에도 높은 효소활성을 보였다. Casein의 분해속도는 배양 24에서 36시간에서 가장 높았으며, 전기영동을 통한 casein hydrolysis patterns는 ${\alpha}-casein $뿐만 아니라 ${\beta}-casein$도 본 균주에 의해 완전히 분해되었다. 특히 본 균주는 ${\beta}-casein$의 분해력이 더욱 우수하였다.

• Asian-Australasian Journal of Animal Sciences
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• 제8권2호
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• pp.187-194
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• 1995

Genetic variants of ${\alpha}s_1$-casein, ${\beta}$-casein, ${\kappa}$-casein and ${\beta}$-lactoglobulin were investigated by starch urea gel electrophoresis in milk samples of 280 Korean native cattle. A new ${\beta}$-casein variant, designated ${\beta}$-casein $A^4$, was found in milk samples of Korean native cattle. It has a much slower electrophoretic mobility than the ${\beta}$-casein $A^3$ variant in acid gel. This new variant appeared together with either ${\beta}$-casein $A^1$, $A^2$ or B variant. Gene frequencies and genotypic frequencies were estimated. Gene frequencies of four milk protein loci in Korean native cattle were compared with those of imported cattle breeds raised in Korea and Japanese brown cattle. Gene frequencies were ${\alpha}s_1$-casein B .846, ${\alpha}s_1$-casein C .154; ${\beta}$-casein $A^1$ .216, ${\beta}$-casein $A^2$ .666, ${\beta}$-casein $A^4$ .048, ${\beta}$-casein B .070; ${\kappa}$-casein A .648, ${\kappa}$-casein B .352; ${\beta}$-lactoglobulin A .148, ${\beta}$-lactoglobulin B .852. The population was in Hardy-Weinberg equilibrium at all milk protein loci. Gene frequencies of Korean native cattle were very similar to those of Japanese brown cattle. Interestingly, a new variant, ${\beta}$-casein $A^4$, was found only in Korean native cattle and Japanese brown cattle. These results support the hypothesis that Korean native cattle were used in the development of the Japanese brown cattle.

• Journal of Dairy Science and Biotechnology
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• 제41권3호
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• pp.149-156
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• 2023

Milk protein is often fractionated/concentrated by using various techniques in dairy industries. Among these techniques, ultrafiltration (UF) is particularly efficient at concentrating the casein fraction of milk protein. The objectives of this study were to produce casein hydrolysates by concentrating the casein fraction in skim milk using the UF technique and to investigate the chemical composition of the casein hydrolysates. The skim milk was concentrated using a UF laboratory test unit equipped with 10 kDa and 30 kDa membranes. After UF, the protein content of the milk was concentrated up to ~7.2% and the Ca was concentrated up to ~196 mg/100 g of milk. Trypsin was then added to the concentrated skim milk to produce the casein hydrolysates. The results of sodium dodecyl sulphate-polyacrylamide gel electrophoresis showed that the casein fraction was not present after hydrolysis, indicating that casein in the milk had been hydrolyzed. The Ca content in the casein hydrolysates was much higher (p<0.05) compared to Ca content in commercial casein phosphopeptides (CPP) indicating that was acidified during the manufacture of commercial CPP. In conclusion, it seems that casein hydrolysates containing large concentrations of protein and Ca can also be made from concentrated UF milk without acidification or renneting.

• Journal of Dairy Science and Biotechnology
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• 제14권2호
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• pp.135-146
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• 1996

본 연구는 UF에 의한 cheese base제조과정 중 calf rennet 과 대용효소인 porcine pepsin을 각각 단독, 또는 1:1로 혼합첨가하여 cheese base를 제조한 후, HPLC와 전기영동을 이 용하여 casein의 변화를 관찰하기 위여 실시하였으며 얻어진 결과는 다음과 같다. HPLC를 이용, Superose 12 column에 의하여cheese casein을 gel filtration한 결과, Cheddar cheese는 제조직후 5개의 분획이었던 것이 6개월 숙성후 8개의 분획으로 분별되었으며, 효소처리하지 않은 대조구 cheese base는 8주 숙성중 4개의 분획으로 분별되어 분획수의 큰 변동은 없었고, calf rennet 단독처리구는 4개에서 5개로, 1:1혼합효소처리구(calf rennet : porcine pepsin)는 4개에서 7개로, porcine pepsin 단독처리구는 4개에서 8개로 각각 분별되어 porcine pepsin이 혼합됨에 따라 casein의 분해 정도가 높았다. 효소처리하여 8주간 숙성시킨 cheese base의 casein을 전기영동한 결과, ${\alpha}$$_{s1}$-casein의 경우, calf rennet 단독처리구는 3개의 band로 분리되었고, 1:1혼합효소처리구(calf rennet :porcine pepsin)와 Porcine pepsin 단독처리구는 5개의 band로 분리되었으며, 대조구는 1개의 major band와 2개의 minor band를 나타내었다. ${\beta}$-casein은 porcine pepsin의 첨가비율이 증가할수록 그 농도는 감소하였고, ${\gamma}_1$ ${\gamma}_2$-casein으로 추정되는 band는 상대적으로 증가함을 나타내었다. 또한 para-${\kappa}$-casein은 대조구를 제외하고 calf rennet, porcine pepsin단독처리구, 1:1혼합효소처리구에서 분리되었다.

• 한국식품영양과학회지
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• 제26권6호
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• pp.1102-1108
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• 1997

Proteins and polysaccharides confer distinct functional properties in food systems. This research was attempted to improve emulsion properties of casein by protein-polysaccharide conjugation, in which alginates with various molecular weights were employed as polysaccharide sources. Casein-alginate mixtures were conjugated by the amino-carbonyl or Maillard reaction at 6$0^{\circ}C$ and 79% relative humidity. The resulting casein-alginate conjugates were tested for their emulsion activity and emulsion stabilizing properties. In general, the emulsion stability of casein-alginate mixture greatly increased due to the amino-carbonyl reaction between casein and alginates, whose magnitude depended on the molecular weight of alginate, weight ratio of casein to alginate and incubation time. It was also found that thermal stability and pH stability were markedly improved by the casein-alginate conjugation.

• Journal of Microbiology and Biotechnology
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• 제1권1호
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• pp.31-36
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• 1991

Yeast expression plasmids containing an appropriate leader sequence and bovine $\beta$-casein cDNA were constructed to produce $\beta$-casein for the study of its functional characteristics. Two kinds of expression systems for $\beta$-casein were constructed using pCGYl444 as a precursor plasmid. This plasmid is a yeast-E. coli shuttle vector which contains the chelatin promoter. The plasmid pISB202 contains the invertase leader sequence and $\beta$-casein gene. The plasmid pDEB303 contains the original bovine $\beta$-casein leader sequence gene. These two plasmids were introduced into S. cerevisiae AB116 which is a strain deficient in the major yeast proteinases. Each clone was grown in minimal media for 24 h before induction by $CuSO_4$. The cells were thus grown under expression conditions. Both strains harbouring pISB202 and pDEB303 expressed bovine $\beta$-casein. The $\beta$-casein was detected using immunochemical staining after western blot. Secretion of $\beta$-casein was detected in the culture broth. The estimated amount of secreted $\beta$-casein was approximately 50 ${\MU}g$/l.

• 운동영양학회지
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• 제24권2호
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• pp.6-10
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• 2020

[Purpose] Milk is a commonly ingested post-exercise recovery protein source. Casein protein, found in milk, is characterized by its slow digestion and absorption. Recently, several studies have been conducted with a focus on how pre-sleep casein protein intake could affect post-exercise recovery but our knowledge of the subject remains limited. This review aimed at presenting and discussing how pre-sleep casein protein ingestion affects post-exercise recovery and the details of its potential effector mechanisms. [Methods] We systematically reviewed the topics of 1) casein nutritional characteristics, 2) pre-sleep casein protein effects on post-exercise recovery, and 3) potential effector mechanisms of pre-sleep casein protein on post-exercise recovery, based on the currently available published studies on pre-sleep casein protein ingestion. [Results] Studies have shown that pre-sleep casein protein ingestion (timing: 30 minutes before sleep, amount of casein protein ingested: 40-48 g) could help post-exercise recovery and positively affect acute protein metabolism and exercise performance. In addition, studies have suggested that repeated pre-sleep casein protein ingestion for post-exercise recovery over a long period might also result in chronic effects that optimize intramuscular physiological adaptation (muscle strength and muscle hypertrophy). The potential mechanisms of pre-sleep casein protein ingestion that contribute to these effects include the following: 1) significantly increasing plasma amino acid availability during sleep, thereby increasing protein synthesis, inhibiting protein breakdown, and achieving a positive protein balance; and 2) weakening exercise-induced muscle damage or inflammatory responses, causing reduced muscle soreness. Future studies should focus on completely elucidating these potential mechanisms. [Conclusion] In conclusion, post-exercise ingestion of at least 40 g of casein protein, approximately 30 minutes before sleep and after a bout of resistance exercise in the evening, might be an effective nutritional intervention to facilitate muscle recovery.