Journal of the Korean Society of Food Science and Nutrition (한국식품영양과학회지)
- Volume 13 Issue 2
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- Pages.193-204
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- 1984
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- 1226-3311(pISSN)
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- 2288-5978(eISSN)
Enzymological Properties of the Alkaline AL-Protease from Arthrobacter luteus and Detection of Its Active Amino Acid Residue
Arthrobacter luteus로부터 유래한 염기성 AL-Protease의 효소학적 성질 및 활성 아미노산 잔기의 검색
- Oh, Hong-Rock (Dept. of Animal Science, Chungnam National University) ;
- Aizono, Yasuo (Dept. of Agricultural Chemistry, Kyushu University) ;
- Funatsu, Masaru (Dept. of Applied Microbial Technology, The Kumamoto Institute of Technology)
- Published : 1984.06.30
Abstract
The enzymatic properties of the alkaline AL-protease, which had been prepared from the crude zymolyase of Arthrobzoter luteus, was investigated together with its active amino acid residue. Complete inactivaton of the proteolytic activity of AL-protease by either DFP or PMSF was simultaneously accompanied by the loss of its lytic effect on the lysis of yeast cell wall. In the reaction, AL-protease showed the pattern of inactivation to decrease very slowly, as compared to that of chymotrypsin, and that enzyme and DFP were found to react with a molar ratio of 1 : 1. The preparation of AL-protease exhibited no hydrolytic activity in any substrates of polysaccharases, playing a significant role in the lysis of yeast cell wall. The optimum pH and temperature of AL-protease was pH 10.5 and
Zymolyase 조효소로부터 분리, 정제되었고, 효모세포벽 용해 촉진물질로 밝혀진 바 있는 Arthrobacter luteus로부터 유래한 염기성 protease(AL-protease)의 효소학적 성질 및 활성 아미노산 잔기를 검색한 결과는 다음과 같다. 1. AL-pretense는 저해제 DFP 및 PMSF에 의해서 그 Protease 활성 및 용해 촉진활성이 동시에 완전히 소멸 되었으며, 그 저해 반응속도는 chymotrypsin에 대한 것에 비하여 대단히 완만하였다. 1.반응에서 AL-protease와 DFP의 결합 mole비는 1:1로 추정 되었다. 2. 정제된 AL-protease의 동결건조품 중에는 종래효모세포벽 용해반응에 관여하는 것으로 알려진 yeast phosphomannase를 비롯한 다당류 가수분해효소들의 활성은 그 어느 것도 인정되지 않았다. 3. AL-protease의 casein에 대한 최적 pH 및 최적 온도는 pH 10.5와
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