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      • Mucor spp L42 응유효소(凝乳酵素)의 고정화(固定化)에 관한 연구

        박종래,이준염,고영숙 한국낙농학회 1986 韓國酪農學會誌 Vol.8 No.3

        精製된 Mucor SPP L_(42) 凝乳酵素을 DEAE-cellulose, CM-cellulose, Sepharose 4-B와 porous glass beads의 四種의 支技劑를 使用하여 各各 다른 方法으로 固定化시킨 후 그 結果를 서로 比較하고, porous glass beads에 固定化시킨 Mucor app L_(42) 凝乳酵素의 性質을 調査하였던 바 그 結果를 要約하면 다음과 같다. 1. 乾燥된 各各의 支技劑에 結合된 酪素蛋白質의 量은 DEAE-cellulose에 24㎎, CM-cellulose에 22㎎, Sepharose 4-B에 20㎎, porous glass bead에 40㎎이었다. 2. 溶解狀態의 酵素蛋白質 10㎎에 대한 支技劑에 結合된 酵素蛋白質 10㎎의 헤모글로빈 分解力의 比率은 DEAE-cellulose는 23, CM-cellulose는 23, Sepharose 4-B는 24, Porous glass bead가 40으로 나타났다. 3. Porous glass bead에 結合된 Mucor spp L_(42) 凝乳酵素의 利用될 수 있는 pH와 溫渡에 대한 範位가 溶解性諸素에 비하여 넓어진 것으로 나타났다. Mucor spp. L_(42) milk-clotting enzyme was coupled to DEAE-cellulose, CM-cellulose, Sepharose 4-B and porous glass bead by different methods respectively. Amount of enzyme attatched to the matrixes was analysed by micro kjeldahl method. Activity of individual immobilized enzyme was compared to native enzyme. Properties of the immobilized Mucor spp. L_(42) milk-clotting enzyme on succinamidopropyl glass bead with glutaraldehyde were tested. The results abtained were summerized as follow. 1. Amount of enzyme attatched to one gram of individual dried beads was mg for DEAE-cellulose, mg for CM-cellulose, mg for Sepharose 4-B and mg for porous glass bead respectively. 2. Ratio of activity for 10mg of enzyme attatched on individual beads to 10mg on individual native enzyme was for DEAE-cellulose, for CM-cellulose, for Sepharose 4-B and for porous glass bead. 3. Ranges of available pH and temperature for immobilized Mucor spp L_(42) milk-clotting enzyme to succinamidopropyl glass bead were improved than soluble one.

      • KCI우수등재

        인유 단백질에 대한 연구

        박종래,김영주,이상렬 ( J . L . Park,Y . J . Kim,S . Y . Lee ) 한국축산학회 1974 한국축산학회지 Vol.16 No.3

        Human milk sample was taken from 15 women living Sumon, Korea who are in the stage of 1 to 3 month after pasturition and its chemical composition, amino acids content and electrophoretical mobility were studied. The milk contained 2.36±0.66% of fat, 1.30±0.16% of protein, 7.25±0.34% of lactose and 0.12±0.03% of ash, and the ratio of casein to whey protein was 1 : 1.3. Human acid casein contained more amino acids such as Glu, Val, Ileu, and Leu but less amount of Ser, and Pro than that of Holstein milk. As human casein was analyzed for electrophoretic movibility, four main electrophoretic bands were formed at the position of bovine k-casein and no band was appeared at the position of bovine αs-casein when 6% polyacrylamide gel and tris-EDTA buffer pH 8.6 were used. Human whey protein did not appear at the position of bovine β-lactoglobulin while a large amount of lactoferrin was observed from the position of bovine immunoglobulin.

      • KCI우수등재

        Mucor L42 의 응유효소 생산에 관한 연구

        박종래,김현욱,김영주 ( Jong Lae Park,Hyun Uk Kim,Young Ju Kim ) 한국축산학회 1979 한국축산학회지 Vol.21 No.2

        Mucor L_(42), isolated as the milk clotting enzyme producing fungi in this laboratory, has been extensively tested for optimum medium compositions and optimum growth conditions for the enzyme production and the results obtained could be summarized as follows, 1. The best enzyme production media known contained 83% of wheat bran, 5.4% of potato starch, 3 % of dextrose, 6.0% of skimmilk powder and 0.5% of ammonium sulfate in the same amount of water as total solid. 2. The optimum mineral contents in the media w as known to be 0.025% of MgSO₄·7H₂O, 0.025% of CaCl₂, 0.05% of MnCl₂, 0.025% of FeSO₄·7H₂O and 0.05 of ZnSO₄·7H₂O. 3. The organism produced the most amount of enzyme at 30℃ in 24 hours in the above medium of pH 6.8

      • 고정화 Mucor SPP L42 응유효소를 이용한 치즈커드 형성에 관한 연구

        박종래 慶北大學校 農業科學技術硏究所 1988 慶北大農學誌 Vol.6 No.-

        활성화시킨 Succinylaminopropyl glass beads에 glutaraldehyde을 사용하여 고정화시킨 Mucor spp L42 응유효소를 치즈 커드 형성과정에 이용하고져 고정화 효소의 안정성, 재이용성, 반응의 조건, 반응조의 형태등에 대하여 탈지유(pH 5.6, 8℃)를 사용하여 반응시킨후 30℃ 항온수조내에서 커드의 형성 상태를 조사하였던바 다음과 같은 결과를 얻었다. 1) 고정화 Mucor spp L42 응유효소를 0.2M phosphate buffer(pH 4.6)에 0.06% sodium azide을 첨가한 액에 침지한 상태로 5℃ 이하에서 보존할 경우 3개월 후에도 활력의 80%가 유지되었다. 2) 고정화 Mucor spp L42 응유효소를 탈지유(pH 5.6, 8℃)로 반응시켰을때 반응 초기에는 고정화 효소의 활력이 급격히 감소하였고, 이것은 bead에 결합되는 질소화합물과 효소의 활력간에 관계가 있는 것으로 나타났다. 3) 고정화 Mucor spp L42 응유효소에 bead와 탈지유의 접촉시간을 60 sec/ml로 하여 탈지유(pH 5.6, 8℃)로 연속적으로 반응시켰을때 6시간 이후에도 bead의 활력의 70%가 유지할 수 있었다. 4) Fluidized bed와 shaking fluidized bed을 사용하는 것이 충진반응조 보다 탈지유의 반응속도가 높았다. In order to study of practical purpose of immobilized Mucor spp L42 milk clotting enzyme on activated succimylamino-propyl glass beads with glutaraldehyde in continuous curd coagulation, acidified milk(pH5.6,8℃) was treated through reactor packed with immobilized beads, and warmed at 30℃ and allowed to coagulation for the determination of enzyme stability, deactivation of milk clotting ability by continuous reaction, the beads treatment conditions, and contact time of milk and beads in reactors. The results obtained were summarized as follow; 1) After 3 month's storage, activity of immobilized Mucor spp L42 milk clotting enzyme in 0.2M phosphate buffer(pH 4.6) with 0.06% sodium azide was only 80% of initial activity. 2) Milk clotting activity of the beads was decreased by continuouse exposure on acidified skim milk. Nitrogen accumulation on the beads paralled loss of the activity in initial reaction stage. 3) After 6 hours continuous treatment of the beads at 60 sec/ml surface time, the milk-clotting activity of the beads was about 70% of initial activity. 4) Bead reactor and shaking bed reactor were more effective than column reactor on continuouse skim milk coagulation.

      • KCI우수등재

        표면처리가 Torayca T300 탄소섬유의 Morphology 및 역학적 거동에 미치는 영향

        박종래,임순호,Park, Jong-Rae,Im, Sun-Ho 한국섬유공학회 1996 한국섬유공학회지 Vol.33 No.11

        The effect of surface treatment at high temperatures on the morphology and mechanical behavior of Torayca T300 carbon fiber is studied. It is found that the surface treatment results in a considerable change in the surface and cross-sectional morphology of the carbon fiber. Accordingly, there are sizable change in mechanical properties of the fiber: in particular, compressional failure mechanism changes from buckling to simple shear mode as the surface treatment temperature increases. There is not an apparent relationship between the surface structural parameters such as surface area, pore volume, etc. and the mechanical properties such as tensile and compressive strengths.

      • KCI우수등재

        Cheddar Cheese 숙성과정에 있어서 Casein 의 변화

        박종래,김영주,송계원 ( J . L . Park,Y . J . Kim,K . W . Song ) 한국축산학회 1975 한국축산학회지 Vol.17 No.2

        To study the change of cheese casein components during the ripening of cheddar cheese, the fresh cheese was ripened for 6 monthes at 10±2℃, 90±5% of relative humidity(R.H), water soluble nitrogen and noneprotein nitrogen(N.P.N), polyacrylamide gel-electrophoretic patterns, DEAF-cellulose chromatographic fractions, sephadex gel-filtration, and the content of free amino acids, were studied during the ripening of the cheese at the Laboratory of Dairy Chemistry, Livestock Experiment Station in Suwon, Korea. The results obtained were as follows: (1) Water soluble nitrogen was 28%, 39%j and 59% of total nitrogen and N.P.N. was 9% 17%, and 22% of total nitrogen at 4th week, 12th week and 24th week of chose ripening, respectively. (2) On 6% polyacrylamide gel containing 8M urea and β-mercaptoethanol, electrophoporetic patterns of cheese casein, evidenced 3, 9, 12 bands at the initial, 4th week and 12th week of cheese ripening, respectively. The casein in the cheese aged for 4 weeks was separated into 3 bands, such as α_(s1)-casein, α_(s1)-1-casein. and α_(s1)-2-casein, in the α_(s1)-casein area. The cheese casein aged for 12 weeks evidenced only 2 bands, such as α_(s1)-2-casein and α_(s1)-3-casein with the disappearence of α_(s1)-casein and α_(s1)-1-casein in the α_(s1)-area, and was separated into 4 bands, such as β-casein, β-1-casein, β-2-casein and β-3-casein in the β-casein area. A number of minor bands appeared in the lower descending mobility area than β-casein. It would mean that α_(s1)-casein was degraded earlier than β-casein in cheese ripening. (3) Aged cheese casein in the DEAE-cellulose column(2.5×40㎝) with 0.02M Phospate buffer and 0.3-N. NaCl in 0.02M phosphate buffer, was separated into 4, 8 and 11 protein peaks at the initial, 4th week and 8th week of cheese aging, respectively. (4) The casein of 12 weeks old cheese was separated better and was diffused wider in sephadex G-50 than in sephader G-200, and fresh cheese was separated better and the diffusion was wider in sephadex G-200 than in sephadex G-50. The cheese casein probably were degraded into smaller proteins by rennet and other proteases from lactic bacteria during cheese fermentation. (5) In the cheese aged for 12 weeks many free amino acids appeared, and a number of unknown peaks were found, such as X₁, X₂ and X₃.

      • COMPUTER시대의 남과 여

        박종래 漢陽大學校文理科大學 化學科 1974 化脈 Vol.- No.4

        ※연구실 비신사록 어느 미국서적에 화학적 분석에 관하여 다음과 같은 풀이가 쓰여 있었다. 여성의 화학적 분석 기호:WM 원자량:약 110lb 소재:남성이 있는 곳에는 어느 곳에나 존재한다. 물리적성질:STP하에서 아무 반응이 없는데 들끊는 반면에 불시에 굳어져 움지이지 않게 되기가 쉽다. 적당하게 다루면 곧 녹으며 잘 사용하지 않으면 쓴맛이 난다. 화학적 성질:대단히 활발하다. Pt,Au.Ag 및 Diamond에 대하여 친화력이 매우 강하다. 비싼음식을 다량으로 흡수할 수 있으며 홀로 내버려 두면 강렬한 반응을 보인다. 잘생긴 표본옆에 놓으면 색이 새파랑게 변하고 빨리 노화한다. 용도:고도로 장식적이다. 저하된 사기를 앙양하는데 강심제로 사용된다. 재화의 분포를 균등케 하여 지금까지 알려진 가운데서 가장 강력한 수입환원 작용제라고 할 수 있다. 주의: 경험이 부족한 손으로 다룰 때는 극히 폭발성이 크다

      • KCI우수등재

        응유효소를 생성하는 곰팡이에 대한 연구

        박종래,김현욱,김영주 ( Jong Lae Park,Hyun Uk Kim,Young Ju Kim ) 한국축산학회 1979 한국축산학회지 Vol.21 No.2

        Samples of soil, hay, koji, animal manure have been extensively tested to obtain a fungal strain which would produce milk clotting enzyme efficiently. Among 16 fungal isolates, Isolate L_(42) was the most potent producer of milk clotting enzyme when cultured in wheat bran medium. Based on the limited information, we presumptively identify this isolates as Mucor spp. L_(42)

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