Enzymatic decolorization of textile dyeing effluents

Commercial azo, triarylmethane, antraquinonic, and indigoid textile dyes are efficiently decolorized with enzyme preparations from Pleuratus ostreatus, Schizophyllum commune, Neurospora crassa, Polvporus sp., Sclerotium rolfsii, Trametes villosa, and Myceliophtora thermophila. The nature of substituents on the dyes' benzene rings influences enzyme activity, and hydroxyl and amino groups enhance decolorization. The presence of lignin peroxidase and/or manganese peroxidase in addition to Iaccase (P. Ostreatus, S. commune, S. rolfsii, N. crassa) increases decolorization by up to 25%, The effect of textile dyeing auxiliaries depends on the individual enzymes. Polyporus sp. and T. villosa are inhibited up to 20% by copper and iron chelating agents and anionic detergents, while the S. Commune enzymes lose up to 70% of their activity

Characterization of Human Alpha-Dystrobrevin Isoforms in HL-60 Human Promyelocytic Leukemia Cells Undergoing Granulocytic Differentiation

The biochemical properties and spatial localization of the protein alpha-dystrobrevin and other isoforms were investigated in cells of the human promyelocytic leukemia line HL-60 granulocytic differentiation as induced by retinoic acid (RA). Alpha-dystrobrevin was detected both in the cytosol and the nuclei of these cells, and a short isoform (gamma-dystrobrevin) was modified by tyrosine phosphorylation soon after the onset of the RA-triggered differentiation. Varying patterns of distribution of alpha-dystrobrevin and its isoforms could be discerned in HL-60 promyelocytes, RA-differentiated mature granulocytes, and human neutrophils. Moreover, the gamma-dystrobrevin isoform was found in association with actin and myosin light chain. The results provide new information about potential involvement of alpha-dystrobrevin and its splice isoforms in signal transduction in myeloid cells during induction of granulocytic differentiation and/or at the commitment stage of differentiation or phagocytic cells