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KMID : 0379120080360020183
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Korean Journal of Mycology
2008 Volume.36 No. 2 p.183 ~ p.188
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Characterization of a Fibrinolytic Serine Protease from an Edible Mushroom, Albatrellus confluens
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Kim Jun-Ho
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Abstract
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A fibrinolytic serine protease was purified from the fruiting bodies of an edible mushroom, Albatrellus confluens. The enzyme had a molecular mass of 30086.41 Da, as measured by MALDI-TOF mass spectrometry. The N-terminal amino acid sequence of the enzyme was Glu-Thr-Val-Thr-Glu-Thr-Thr-Ala -Pro-Trp-Gly-Leu-Ser-Arg-Ile. It displayed optimal activity at and within a pH range of , suggesting that the enzyme is an alkaline protease. The enzyme was stable up to . The enzyme displayed a strong substrate specificity for the synthetic peptide, N-Suc-Ala-Ala-Pro-Phe pNA. The enzyme activity was completely inhibited by addition of PMSF, indicating that the enzyme is a serine protease. No inhibition was observed following addition of E-64, pepstatin, or EDTA. The activity of the purified enzyme was decreased in the presence or , and the enzyme was completely inhibited by addition of . From these results, we propose that Albatrellus confluens could be used for biofunctional foods development and has potential therapeutic value for the treatment of vascular diseases.
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KEYWORD
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Albatrellus confluens, Fibrinolytic serine protease, Vascular diseases
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