In:
Journal of Biomedicine and Biotechnology, Hindawi Limited, Vol. 2012 ( 2012), p. 1-8
Abstract:
A novel 68 kDa laccase was purified from the mycorrhizal fungus Agaricus placomyces by utilizing a procedure that comprised three successive steps of ion exchange chromatography and gel filtration as the final step. The monomeric enzyme exhibited the N-terminal amino acid sequence of DVIGPQAQVTLANQD, which showed only a low extent of homology to sequences of other fungal laccases. The optimal temperature for A. placomyces laccase was 30°C, and optimal pH values for laccase activity towards the substrates 2,7′-azinobis[3-ethylbenzothiazolone-6-sulfonic acid] diammonium salt (ABTS) and hydroquinone were 5.2 and 6.8, respectively. The laccase displayed, at 30°C and pH 5.2, K m values of 0.392 mM towards hydroquinone and 0.775 mM towards ABTS. It potently suppressed proliferation of MCF 7 human breast cancer cells and Hep G2 hepatoma cells and inhibited human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) activity with an IC 50 of 1.8 μ M, 1.7 μ M, and 1.25 μ M, respectively, signifying that it is an antipathogenic protein.
Type of Medium:
Online Resource
ISSN:
1110-7243
,
1110-7251
Language:
English
Publisher:
Hindawi Limited
Publication Date:
2012
detail.hit.zdb_id:
2698540-8
detail.hit.zdb_id:
2512507-2
SSG:
12
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