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KMID : 0366119730010020093
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Korean Journal of Applied Microbiology & Bioengineering
1973 Volume.1 No. 2 p.93 ~ p.98
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Studids on the acid stable protease from Penicillium sp.
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Abstract
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The acid protease was isolated from the culture broth of the Penicillum sp. grown in the wheat bran media. "The crude purification of this enzyme was carried out by extraction with distilled water and precipitated with saturated ammonium sulfate." The activity of this enzyme was found to be very strong by Folin´s colorimetric method. The results were as follows.
1. The optimum pH of the enzyme activity was at 3. 0 and its optimum temperature was 50℃.
2. Although the enzyme activity to hydrolyze casein was maximal at 50℃, its activity decreased rapidly by about 50%, treated at 50℃ for 30 min. When treated at 40℃ for 60
the enzyme activity decreased to 75% of original value and did not decrease any more.
3. The enzyme was stable at pH 2.0 to 6.0.
4. This enzyme activity was not effected by metal ions; Cd^(++), Zn^(++), Co^(++), Hg^(++), Mn^(++), Pb^(++), Mg^(++), Li^(+), Cu^(++), Ba^(++), Ag^(+), Al^(+++), Ca^(++), Fe^(++), and Fe^(+++).
5. Also, it was not effected by treatemnt of EDTA.
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