title: Lytic enzyme activity in autolysing mycelium of Aspergillus niger.
abstract: We have studied changes in the activity of some lytic enzymes contained in mycelium of Aspergillus niger in cultures relative to the autolytic phase of growth. Acid phosphatase, polygalacturonidase and alpha-amylase activity reached its highest level (40.7, and 8 U/sample, respectively) at the initiation of the autolytic phase of growth. 1.3-beta-Glucanase and beta-N-acetylglucosaminidase reached its highest level (3.5 and 2 U/sample, respectively) during the first days of autolysis. Alkaline phosphatase, cellulase, invertase, esterase, chitinase and proteolytic activity is also present in autolysing mycelium of A. niger, though comparatively low. Their maximum activity coincided with the beginning of the autolytic phase of growth. In all enzymes studied here, as autolyis proceeded, enzyme activity decreased by about 90%. Only esterase activity remained nearly constant throughout the whole period of autolysis described here.
mesh_terms: D000118:Acetylglucosaminidase / Q000378:metabolism; D000135:Acid Phosphatase / Q000378:metabolism; D001234:Aspergillus niger / Q000201:enzymology* / Q000502:physiology; D043326:Glucan 1,3-beta-Glucosidase; D005959:Glucosidases / Q000378:metabolism; D006867:Hydrolases / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism; D011096:Polygalacturonase / Q000378:metabolism; D013997:Time Factors; D000516:alpha-Amylases / Q000378:metabolism
chemical_list: D006867:Hydrolases; D000135:Acid Phosphatase; D005959:Glucosidases; D000516:alpha-Amylases; D011096:Polygalacturonase; D000118:Acetylglucosaminidase; D043326:Glucan 1,3-beta-Glucosidase; D010447:Peptide Hydrolases