Purification and characterization of two novel fibrinolytic proteases from mushroom, Fomitella fraxinea

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dc.contributor.authorJong Suk Lee-
dc.contributor.authorH S Baik-
dc.contributor.authorS S Park-
dc.date.accessioned2017-04-19T09:04:14Z-
dc.date.available2017-04-19T09:04:14Z-
dc.date.issued2006-
dc.identifier.issn10177825-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/7347-
dc.description.abstractTwo fibrinolytic enzymes were purified from the culture supernatant of Fomitella fraxinea mycelia by ion-exchange and gel filtration chromatographies, and were designated as F. fraxenia proteases 1 and 2 (FFP1 and FFP2). The apparent molecular masses of the enzymes were estimated to be 32 kDa and 42 kDa, respectively, by SDS-PAGE and gel filtration chromatography. Both enzymes had the same optimal temperature (40°C), but different pH optima (10.0 and 5.0 for FFP1 and FFP2, respectively). FFP1 was relatively stable at pH 7.0-9.0 and temperature below 30°C, whereas FFP2 was very stable in the pH range of 4-11 and temperature below 40°C. FFP1 activity was completely inhibited by phenylmethylsulfonyl fluoride (PMSF) and aprotinin, indicating that this enzyme is a serine protease. The activity of FFP2 was enhanced by the addition of Co2+ and Zn2+ and inhibited by Cu2+, Ni2+, and Hg2+. Furthermore, FFP2 activity was strongly inhibited by EDTA and 1,10-phenanthroline, implying that the enzyme is a metalloprotease. Both enzymes readily hydrolyzed fibrinogen, preferentially digesting the Aα- and Bβ-chains of fibrinogen over γ-chain. FFP1 showed broad substrate specificity for synthetic substrates, but FFP2 did not. Km, and Vmax values of FFP1 for a synthetic substrate, N-succinyl-Ala-Ala-Pro-Phe-pNA, were 0.213 mM and 39.68 units /ml, respectively. The first 15 amino acids of the N-terminal sequences of both enzymes were APXXPXGPWGPQRIS and ARPP(G)VDGQ(R,I)SK(L)ETLPE, respectively.-
dc.publisherSouth Korea-
dc.titlePurification and characterization of two novel fibrinolytic proteases from mushroom, Fomitella fraxinea-
dc.title.alternativePurification and characterization of two novel fibrinolytic proteases from mushroom, Fomitella fraxinea-
dc.typeArticle-
dc.citation.titleJournal of Microbiology and Biotechnology-
dc.citation.number2-
dc.citation.endPage271-
dc.citation.startPage264-
dc.citation.volume16-
dc.contributor.alternativeName이종석-
dc.contributor.alternativeName백형석-
dc.contributor.alternativeName박상신-
dc.identifier.bibliographicCitationJournal of Microbiology and Biotechnology, vol. 16, no. 2, pp. 264-271-
dc.subject.keywordcharacterization-
dc.subject.keywordfibrinolytic protease-
dc.subject.keywordfomitella fraxinea-
dc.subject.keywordmetalloprotease-
dc.subject.keywordpurification-
dc.subject.keywordserine protease-
dc.subject.localcharacterization-
dc.subject.localCharacterization-
dc.subject.localfibrinolytic protease-
dc.subject.localfomitella fraxinea-
dc.subject.localFomitella fraxinea-
dc.subject.localmetalloprotease-
dc.subject.localpurification-
dc.subject.localPurification-
dc.subject.localserine protease-
dc.subject.localSerine protease-
dc.description.journalClassY-
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