• Korean Journal of Food Science and Technology
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• v.14 no.1
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• pp.49-56
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• 1982

The effects of measurement conditions on the emulsifying capacity(EC) and emulsion stability(ES) of proteins were studied in order to develop laboratory standard methods for the evaluation of emulsifying properties. The EC of proteins decreased with the increments of protein concentration and mixing rate. It increased with the increasing oil addition rate up to 0.8 ml/sec, but did not change at $0.8{\sim}1.2\;ml/sec$. The addition of sodiumchloride enhanced EC of proteins, attaining to the highest EC at 0.3M NaCl for Pro-Fam and 0.1M NaCl for Na-caseinate. The ES of Pro-Fam was higher than that of caseinate. The ES was increased by the increments of protein concentration, oil addition volume, mixing rate and mixing time. The EC and ES showed a close relation to the NSI of proteins, reaching to the lowest values of EC and ES at the isoelectric regions of proteins. The laboratory methods for measurements of emulsifying properties of proteins were established. The emulsifying properties of a laboratory-made soybean protein isolate were compared to those of commercial products by using the methods.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.29 no.4
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• pp.464-473
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• 1996

Two-month feeding experiment was conducted to investigate the optimum dietary protein level and energy to protein ratio in fat cod (Hexagrammos otakii Jordan et STARKS). The fish averaging 29 g were fed with one of the isocaloric diets containing 30, 40, 50 or $60\%$ of protein, or with one of the isoproteic diets containing 9, 10, 11 or 12 of available energy/protein (E/P) ratio. Weight gain and feed efficiency increased significantly with dietary protein level up to $50\%$, then decreased with $60\%$ protein diet (P<0.05). Daily protein intake increased significantly with dietary protein level, whereas protein efficiency ratio decreased with dietary protein level (P<0.05). Second order polynomial regression analyses of percent weight gain and daily protein intake may indicate that the adequate dietary protein level is $45\%$ and daily protein requirement per 100g fish is 1.5g for maximal growth. Weight gain, feed efficiency and protein efficiency from fish led the diet containing 12 of E/P ratio were significantly higher than those from fish fed the other diets (P<0.05). Daily feed or protein intake from fish fed the diet containing 12 of E/P ratio was significantly lower than those from fish fed the other diets (P<0.05). Daily lipid intake increased significantly with dietary E/P ratio (P<0.05).

• Journal of Life Science
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• v.8 no.6
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• pp.627-637
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• 1998

In order to utilize tuna pyloric caeca among fish intestines wasted when treated raw fish in fish processing manufactory, a crude enzyme with high proteolytic activity was extracted and its optimum condition were investigated. An immobilized enzymes also were prepared by adsorption method to enhance thermostability of the crude proteinase. The yield of the crude proteinase was approximately 2.7% on dry basis. The proteolytic activity for casein was 0.54 U/mg protein, for BTEE 1.10 U/mg protein, and for BAEE 2.69 U/mg protein. It was almost similar to that of the commercial trypsin purified. Optimum hydrolysis activity of the crude proteinase was about 80%, as the degree of hydrolysis for casein, at pH 10.0 and 45$^{\circ}C$ for 12 hrs. Also, when the crude proteinase was immobilized on DEAE-Cellulose and chitin, the residual activities remained after 7 days of pre-incubation time were maintained about 90% or more and their thermostabilities were enhanced by about 50%, compared with the native enzyme.

• The Korean Journal of Food And Nutrition
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• v.15 no.2
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• pp.131-136
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• 2002

Protease activity in matured wax gourd sarcocarp was 0.19unit/0.5ml, immatured wax gourd sarcocarp 0.56unit, and matured wax gourd 24.35 unit, immatured wax gourd core 0.35unit. Protease activity in matured wax gourd sarcocarp to raw meat or raw pork was 13,0 unit, 7.4 unit, respectively, and that in wax gourd core to raw beef was 30.2 unit, and raw pork was 24.5 unit. Thermal stability of pretense in matured wax gourd sarcocarp was stable below 70$\^{C}$ when it was heated for 10 minutes. In case of 80$\^{C}$, the remaining activity was 21%, and at 90$\^{C}$, it was lost entirely. The absorption spectrum showed peak at 280nm. According to the HPLC analysis, casein was hydrolyzed into small size by protease in core or sarcocarp of matured was gourd and immatured wax gourd. Wax gourd diluted by 1/10 showed two peaks, one was from casein being hydrolyzed, and the other was from the increased molecular weight with coagulated casein. On the other hand, the molecular weight didin't increase in immatured wax gourd core diluted by 1/10. The result of dilution of 1/10 showed different pattern from undiluted one, but the peak of sarcocarp in matured wax gourd was 1 and the peak of core in immatured wax gourd was 5, and those of core and sarcocarp of immatured wax gourd were 3 respectively.

• Food Science of Animal Resources
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• v.32 no.5
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• pp.652-658
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• 2012

This study was carried out to identify the ACE (Angiotensin converting enzyme) inhibitory activity of casein hydrolysates for development of anti-hypertensive hydrolysates. Sodium caseinate was treated with six kinds of commercial proteases such as Flavourzyme, Protamex, Neutrase 1.5, Alcalase, Protease M, and Protease S for 8 h individually, and was then treated with the enzyme combination for 4 h at $45^{\circ}C$. The hydrolysate which had the highest ACE inhibitory effect was then hydrolysed successively with three digestive enzymes: pepsin, trypsin, and ${\alpha}$-chymotrypsin, at $37^{\circ}C$ for 4 h under conditions mimicking those of the gastrointestinal tract. UF (ultra filtration) treatment was applied to one of the secondary hydrolysates to determine ACE inhibitory activity. When sodium caseinate was hydrolysed by commercial proteases, the degree of hydrolysis (DH) showed 2.54 to 4.25% and after secondary hydrolysis, DH showed 4.30 to 5.22%. ACE inhibitory activity and $IC_{50}$ values decreased, and inhibition rates increased during hydrolysis. Protamex treatment showed the lowest $IC_{50}$ value ($516{\mu}g/mL$) and Flavourzyme hydrolysate showed the highest $IC_{50}$value ($866{\mu}g/mL$). As the first hydrolysate was treated with Flavourzyme, the ACE inhibitory activity increased. Neutrase hydrolysate had the highest activity with an $IC_{50}$ value ($282{\mu}g/mL$). When Neutrase plus Flavourzyme treatment was hydrolyzed by digestive enzymes, the $IC_{50}$ value ($597{\mu}g/mL$) was decreased statistically (p<0.05). As Neutrase plus Flavourzyme hydrolysate is treated by UF with MW cut-off 10,000, permeate showed $273{\mu}g/mL$ of $IC_{50}$ value, showed no difference, but retentate which has over MW 10,000 showed statistically different $IC_{50}$ value, $635{\mu}g/mL$ (p<0.05).

• Korean journal of food and cookery science
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• v.7 no.4
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• pp.93-101
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• 1991

The object of this study was to investigate characteristics of kiwifruit protesae and effect of this enzyme on the functionality of casein. The specific activity of crudely prepared kiwifruit pretense on casein was 196.95 units/mg protein, it showed optimum activity at pH 3.0, $60^{\circ}C$. The degree of hydrolysis of casein with pretense treatment steeply increased to 73.5% and 78.9% for 10 and 20 minutes and then reached 84.1% and 89.3% for 1 and 4 hours, respectively. Solubility of non heated control group was 0.2% at pH 4, while the sample groups treated with enzyme for 0, 10 and 20 minutes were 14.5%, 19.2% and 24.0%, respectively. Casein treated with pretense showed marked increase in foam expansion near isoelectric point. However, enzymatically treated groups had lower foam expansion than the control groups. Foam stabilities of enzymatically modified group were lower than those of the control groups at all pH. Emulsifying activity of the non-heated control group was 0% at pH 4, while the groups modified enzymatically for 0, 10, and 60 minutes showed 51.0%, 55.5% and 54.5%, respectively.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.18 no.10
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• pp.551-558
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• 2017

To study and validate tissue-specific promoters and vectors, it is important to develop cell culture systems that retain the tissue and species specificity. Such systems are attractive alternatives to transgenic animal models. This study established a line of porcine mammary gland epithelial cells (PMECs) from a primary culture based on the cellular morphology and mRNA levels of porcine beta-casein (CSN2). The selected PMECs were stained with the cytokeratin antibody, and were shown to express milk protein genes (CSN2, lactoferrin, and whey acidic protein). In addition, to confirm the acini structure of PMEC932-7 in 3D culture, live cells were stained with SYTO-13 dye, which binds to nucleic acid. The acini of these PMECs on matrigel were formed by the aggregation of peripheral cells and featured a hollow lumens. The system was demonstrated by testing the effects of the culture conditions to cell culture including cell density and matrigel methods of the PMECs. These results suggest that PMECs possess the genetic and structural features of mammary epithelial cells.

• Korean Journal of Animal Reproduction
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• v.21 no.1
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• pp.1-7
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• 1997

Recently the production of transgenic animals to express foreign proteins in mammary glands has been a routine procedure. However, it still takes a considerable time and effort, and is faced with various technical challenges until the protein of interest is successfully made. Thus, a development of an a vitro model for mamm a ary-specific gene expression for recombinant genes was carried out in this study. To this end, bovine $\alpha$$_S1$ casein cDNA was inserted at the multiple cloning site of pMSG vector under the control of MMTV promoter. MCF$_7$ cells were tran sfected with pMSG $\alpha$$_S1$ CN by CaP0$_4$ precipitation. Transfectants were selected in HAT medium and induced with dexamethasone. The cells were analyzed with chicken anti-casein and FITC-labeled rabbit anti-chicken antibodies. The results showed that dexamethasone induced 30-40 fold increase in the MMTV- $\alpha$$_S1$ casein e expression. Therefore MCF$_7$ cells, which have multiple steroid receptors, along with pMSG vector can be used as an in vitro model for the study of mammary-specific gene expression.

• Korean Journal of Microbiology
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• v.47 no.3
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• pp.249-254
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• 2011

Mycophenolic acid blocking the synthesis of xanthosine monophosphate is a nonnucleoside inhibitor of inosine monophosphate dehydrogenase. Therefore mycopholoic acid is a drug currently used as immunosuppressive agent in transplantation of heart, kidney and liver. Mycophenolic acid has been industrially produced through fermentation process by fungus Penicillium brevi-compactum. In this study, the profile of mycophenolic acid fermentation was observed in 5L-jar fermentor to investigate the utilization of carbon and nitrogen sources and the production of mycophenolic acid. It was investigated that what kind of carbon sources was better to cell growth and mycophenolic acid production. Fructose was the best carbon source for mycophenolic acid fermentation, but it is the most expensive one. Thereafter molasses containing sucrose as the supply source of fructose was confirmed to be the best carbon source for the industrial production. Use of molasses increased the fermentation yield of mycophenolic acid more than two times higher than glucose. It was confirmed that urea was the best inorganic nitrogen source, which did not give rise to sudden drop of culture pH. Addition of urea increased the fermentation yield of mycophenolic acid about 3.6 times higher than addition of ammonium nitrate as control. Casein, peptone and casamino acid originated from milk protein increased the fermentation yield of mycophenolic acid about 3.4 times higher than control. Peptone and casamino acid, which are casein hydrolysates, increased cell growth considerably as well.

• Journal of Dairy Science and Biotechnology
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• v.32 no.1
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• pp.7-16
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• 2014

Angiotensin-I-converting enzyme (ACE) inhibitory peptides have functional and potential properties of casein hydrolysates that are used in the development of food ingredients and anti-hypertensive hydrolysates derived from sodium caseinate enzymatic hydrolysates. Sodium caseinate could be treated by various kinds of commercial proteases, and then could be treated with the enzyme combination. Ultrafiltration treatment can be used to generate hydrolysates that can be used to determine ACE inhibitory activity. In general, hydrolysate quality can be evaluated by changes in hydrolysis characteristics, ACE inhibitory activity, as well as functional properties such as solubility, foam capacity, cytotoxicity, free radical-scavenging effects, and sensory evaluation. In this review, we present an overview of the ACE inhibitory peptides obtained by performing enzymatic hydrolysis on various sources to identify food ingredients and functional foods that reduce hypertension.