Journal
CHINESE JOURNAL OF CHEMICAL ENGINEERING
Volume 18, Issue 1, Pages 122-128Publisher
CHEMICAL INDUSTRY PRESS CO LTD
DOI: 10.1016/S1004-9541(08)60332-8
Keywords
metalloprotease; Laccocephalum mylittae; purification; characterization; anthelmintic activity
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Funding
- National High Technology Research and Development Program of China [2007AA021506]
- Natural Science Foundation of Zhejiang Province [R207609]
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A neutral metalloprotease was purified from the cultured mycelia of Laccocephalum mylittae, an effective medicinal fungus widely used in anthelmintic therapy The protease was purified to homogeneity with 31.85-fold purification and a final yield of 21.76% The subunit molecular weight of the protease is about 40000 estimated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The optimum reaction pH and temperature are 7 5 and 50 degrees C, respectively The protease activity is largely enhanced by Ca2+, but highly inhibited by tetrasodium ethylenediaminetetraacetate (EDTA), a metal-chelator, suggesting that the enzyme is a metalloprotease The Michaelis-Menten constan K-m and V-max for casein substrate are 6.09 mg ml(-1) and 21.32 mu g min(-1) ml(-1), respectively In vitro anthelmintic tests of the protease exhibit distinct lethal effects on the third stage larvae (L3) of Ascaris suum Scanning electron microscopy and SDS-PAGE analysis indicates that the proteolysis of larvae proteins caused by this protease may relate to the anthelmintic activity of L. mylittae
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