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KMID : 0380219830160030205
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Journal of Biochemistry and Molecular Biology
1983 Volume.16 No. 3 p.205 ~ p.214
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Purification and Properties of Carboxyl Proteinase from the Poria cocos(Schw.) Wolf(Ⅰ)
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Min Tae-Jin
Chung Kwang-Sik
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Abstract
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The enzymic properties of carboxyl proteinase isolated from the Poria cocos(Schw.) Wolf. were investigated. Two kinds of active fractionⅠandⅡ were isolated from this mushroom. The active fractionⅡ showed carboxyl proteinase activity to bovine hemoglobin substrate, and its optimum conditions were the followings temperature, 70℃, pH stability, 1.2∼2.5 and thermal stability, 20˚∼75℃. The enzyme appeared to be one subunit, and consisted of 18 kinds of amino acids. The apparent molecular weight were 25,500(PAGE) and 23,000(HPLC), respectively.
The enzyme appeared to hydrolyze peptide bond between glutaml-L-tyrosine. The Km value of this enzyme was 0.29mM when carbobenzoxy-L-tyrosine were used as a subtrate.
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