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- 저자 : 김영교 ( Yong Il Moon (검색결과 3 건)
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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.
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Mucor miehei Protease 의 이화학적 성질에 관한 연구
김영교,문용일,박동준 한국낙농학회 1984 韓國酪農學會誌 Vol.6 No.2
本 實驗은 casein, 脫脂乳 그리고 유청단백질 등의 기질에 대한 MM protease의 기초적인 理化學的 성질을 파악하기 위하여 NPN定量, 電氣泳動 그리고 凝乳時間測定 등을 실시하였다. 그 결과를 요약하면 다음과 같다. 1. Casein용액(2%)에서 MM protease의 最適 pH는 6.25로 나타났으며, 알칼리상태에서는 급격히 活性이 저하되었다. 2. Casein용액(2%)에서 MM Protease의 最適溫度는 45℃였으며, 60℃까지 완만하게 活性이 떨어지다가 70℃이상에서는 급격히 活性이 저하되었다. 3. 반응시간의 경과에 따라 rennet과는 달리 MM protease는 유리되는 NPN量이 계속 증가하였는데, 초기에는 급속한 증가를 보이다가 2時間 반응 후로는 완만해졌다. 4. 脫脂乳에 CaCl₂를 0.002∼0.01%범위에서 첨가하였을 때, 농도의 증가에 따라서 응고시간도 점점 빨라졌으며, MgSO₄를 0.2∼1.0%범위로 첨가하였을 때에도 응고시간이 발라졌다. 2%이상의 NaCl과 0.002%이상의 CuSO₄의 첨가는 농도가 증가함에 따라 응고를 점점 더 지연시켰다. 5. 유청단백질에 대한 MM protease의 作用을 조사한 결과 유리되는 NPN量은 반응시간의 증가에 따라서 증가하였으나 전기영동상으로는 그 분해받은 정도를 알 수 없었다. 6. Casein용액(2%)에 MM protease와 rennet를 각각 반응시킨 결과 α_s-casein은 MM protease에 의해서 rennet보다 더 분해를 받았으며, β-, κ-casein은 rennet과 거의 비슷한 경향을 나타냈다. 7. MM protease를 전기영동한 결과 κ-casein과 β-casein사이에 단일 band로 나타났다. 8. α_s-casein은 MM protease에 의하여 분해되어 이동도가 빨라졌고, β-casein은 약간 느려졌다. κ-casein은 rennet과 마찬가지로 para-κ-casein의 위치에 단일 band로 나타났다. This experiment was carried out to study the proteolytic activities of Mucor miehei protease by means of polyacrylamide gel electrophoresis, clotting test and quantitative analysis of NPN. The results were summarized as follows: 1. The optimum pH of MM protease activity on 2% casein solution was pH 6.25 and the activity was markedly declined in alkaline phase. 2. The optimum temperature of MM protease activity on proteolysis of 2% casein solution was 45℃ and gradually declined from 45℃ to 65℃ and markedly inactivated above 70℃. 3. The liberation of NPN from 2% casein solution was increased during the 4 hours of incubation. But after the 2 hours of incubation, the increasing rate was lowered. 4. The clotting time of skimmilk was curtailed when the skimmilk contained 0.002 to 0.01% CaCl₂and 0.2 to 0.1% MgSO₄. Conversely, the clotting time was delayed when 2 to 10% NaCl and 0.002 to 0.01% CuSO₄was added. 5. The liberation of NPN from whey protein was increased with incubation time, but the electrophoretic patterns of whey protein before and after the action of MM protease were almost identical. 6. On electrophoresis of the 2% casein solution treated with MM protease, α_χ-casein's degradation was greater than rennet, but the hydrolysis of β- and κ-casein were similar to that of rennet. 7. MM protease was shown as a single band on electrophoresis, and the mobility of MM protease was between β-casein and κ-casein. 8. On electrophoresis of α_s-casein, β-casein and κ-casein treated with MM protease, α_s-casein moved faster than that of original band and β-casein's mobility was lowered, and for κ-casein, it was completely converted into para-κ-casein which moved toward the cathod.
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