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Casein 에 대한 Rennet 및 Streptococcus lactis 의 단백질 분해작용
김영교,O . Kirchmeier ( Yong Kyo Kim ) 한국축산학회 1977 한국축산학회지 Vol.19 No.6
Whole acid casein, α₁-casein and β-casein were treated with St. lactis. rennet, or rennet with St. lactis, respectively, and the degradation of the caseins was detected by the cellulose acetate gel electrophoresis and Sephadex gel filtration. When rennet and St. lactis existed, together in casein solution, proteolytic activity of the enzymes on casein increased markedly compared with the individual action. Under the same conditions, degradation of α₁-casein was much higher than that of β-casein by the proteolytic activity of St. lactis, rennet or rennet with St. Lactic.
치이즈의 숙성에 관한 연구 3 . 체다 치이즈의 수용성질소화합물
김영교 ( Yong Kyo Kim ) 한국축산학회 1976 한국축산학회지 Vol.18 No.2
Water soluble nitrogenous compounds in Cheddar cheese ripened for 4 months were fractionated by Sephadex G-50 column, and the results obtained were summarized as follows. 1. Water soluble nitrogenous compounds were fractionated into 4 fractions and the ratio of F-Ⅰ, F-Ⅱ, F-Ⅲ and F-Ⅳ was 25.8%, 10.00%, 22.80% and 42.12%, respectively. 2. In water soluble nitrogenous compounds, F-Ⅰ and F-Ⅱ were non-dialyzable material, and precipitated in 12% TCA. Un the other hand, F-Ⅲ and F-Ⅳ were dialyzable material, and soluble in 12% TCA. 3. Water soluble nitrogenous compounds showed a few patterns on polyacrylamide gel electrophoresis. 4. Water soluble nitrogenous compounds in ore year old Cheddar cheese made in Australia were fractionated into 3 fractions and no fraction appeared on F-III position. The ratio of F-a, F-b and F-c was 25.10%, 8.44% and 66.46%, respectively.
한우유와 Holstein 종우유의 Casein Micelle 의 성상에 관한 비교연구
김영교(Yong Kyo Kim),황철(C . Hwang) 한국축산학회 1989 한국축산학회지 Vol.31 No.9
This experiment was carried out to compare some properties of casein micelles in Korean native cattle`s milk with those of Holstein cow`s milk. Casein micelles in size were fractionated by ultracentrifugation, and the individual caseins in casein micelles were fractionated by DEAE-cellulose column chromatography. The results obtained were summarized as follows; 1. The total protein contents of Korean cattle`s and Holstein cow`s milks were 4.17% and 3.24%, respectively, and the casein contents of them were 3.27% and 2.57%, respectively. 2. When casein micelles in Korean cattle`s and Holstein cow`s milks were sedimented by centrifugation at 100,000g for 60min, the ratio of micellar casein and serum casein(non-sedimented casein) of the former was similar to that of the latter. However, the relative amount of casein micelles in Korean cattle`s milk precipitated by centrifugation at 100,000g for 10 min was a little lower than that of Holstein cow`s milk. On the other hand, the relative amounts of casein micelles in the former precipitated by centrifugation at 100,000g for 30 and 60min were relatively higher than those in the latter. 3. The relative amount of k-casein in Korean cattle`s milk was slightly higher than that of Holstein cow`s milk, but the amounts of α_s-casein and β-casein of the former were nearly the same with those of the latter. 4. By rennet action, the amount of NPN released from casein of Korean cattle`s milk showed a slightly higher value than that of Holstein cow`s milk, and during the rennet action for 60 min, 5.6% and 3.4% of NPN of the total nitrogen content were released from the former and the latter, respectively. It was, however, observed that there was no difference between both of them on the gel electrophoresis.
문용일(Yong Il Moon),김민배(Min Bae Kim),김영교(Yong Kyo Kim) 한국축산학회 1988 한국축산학회지 Vol.30 No.8
This experiment was carried out to study the proteolytic action of extracellular protease of L. bulgaricus CH-18. Extracellular protease was isolated and purified by means of ammonium sulfate precipitation, DEAE-cellulose column chromatography and Sephadex G-100 gel filtration. The evaluation of molecular weight of the purified extracellular protease was examined by SDS-polyacrylamide gel electrophoresis. The results were summarized as follows: 1. Extracellular protease of L. bulgaricus CH-18 was purified 80.13-fold from supernatant of medium, and yield of activity was 15.48%. 2. The purified extracellular protease was evidenced one band on SDS-polyacrylamide gel electrophoresis, and the molecular weight was calculated to be about 66,500.
장주익,김영교 ( Joo Ick Chang,Yong Kyo Kim ) 한국축산학회 1978 한국축산학회지 Vol.20 No.3
To know the physico-chemical properties of Saanens milk, this experiment has been carried out with Saanens milk collected from Wonju, Kangwon province. Main components and physico-chemical properties of Saanens milk were analyzed. Skim milk, acid caseins and whey proteins obtained from Saanens milk were fractionatd on DEAE-cellulose column. The results were as follows; 1. Total solids, milk fat, proteins, lactose, and ash of Saanens milk were 10.12-13.6% (average 11.61%), 2.3-4.7%(average 3.27%), 3.09-4.36%(average 3.65%), 3.79-4.03%(average 3.91%), and 0.62-0.86%(average 0.78%), respectively. 2. Physico-chemical properties of Saanens milk were 1.026-1.033(average 1.031) in specific gravity, 6.504-7.055(average 6.734) in pH, 0.117-0.193%(average 0.157%) in acidity, positive in alcohol test, and negative in boiling test. 3. Casein percentage, whey protein, lactoglebulin, lactalbumin, soluble nitrogen compounds at 12% TCA(total nitrogen percentage), nitrogen compounds precipitated at 12% TCA (total nitrogen percentage), soluble nitrogen compounds at 3% TCA(total nitrogen percent age), nitrogen compounds precipitated at 3% TCA(total nitrogen percentage) were 1.944%, 1.202 0.156%, 1.046%, 19.31%, 80.69%, 21.36%, and 78.64% respectively. 4. on DEAE-cellulose column, Saanens skim milk was fractionated into 5 fractions, acid casein was fractionated into 4 fractions, and whey protein was fractionated into 5 fractions.
Casein micelle 의 조성에 관한 연구 2 . Casein micelle 의 침전에 대한 온도의 영향
신동철,전우민,김영교 ( Dong Chul Shin,Woo Min Jeon,Yong Kyo Kim ) 한국축산학회 1984 한국축산학회지 Vol.26 No.4
This experiment was carried out to study on the protein composition of casein micelles. Casein micelles were isolated by different temperature of ultracentrifugation. And the composition of individual caseins fur the fractions was determined by DEAF - cellulose column chromatography, The results are summarized as follows: 1. When skimmilk was centrifuged at 4℃, 8.5℃, 13.5℃, 18℃ and 30℃ for 60 min at 200,000 x g, the values for the sedimented casein micelles were 57.80%, 79.79%, 80.85%, 90.43% and 86.88% respectively. 2. When skimmilk was centrifuged for 60 min at 100,000 x g, the values for the sedimented casein micelles and serum casein were 60.85%, and 39.15% at 20℃ and 40.24% and 59.76% at 4℃. 3. The relative amount of αs-, β-, k- and γ-caseins in serum casein which was not sedimented by centrifugation for 60 min at 100,000 x g was 44%, 29%, 19% and 8% at 20℃ and 38%, 34%, 16% and 12% at 4℃ respectively.