Intracellular hydrolases of Aspergillus parasiticus and Aspergillus flavus.
When the distribution profile of hydrolases in mycelial homogenates and culture filtrates of A. parasiticus and A. flavus was examined, six hydrolytic enzymes viz. N-acetyl-beta-glucosaminidase, aryl sulfatase, alkaline proteinase, cathepsin B, cathepsin D and aminopeptidase were detected in homogenate. The culture filtrates were devoid of any activity of these enzymes. The enzyme levels varied with the stage of incubation. The most abundant fungal exopeptidase showing preference for basic amino acid naphthylamides seems to be an aminopeptidase B. Incorporation of CEPA, an ethylene generating compound, stimulated the amino peptidase activity in the mycelium but inhibited the enzyme in vitro. The enzyme was also inhibited by different aflatoxins to varying degree. While aminopeptidase B was located intracellularly, a non-dialysable, heat-stable inhibitor of the enzyme was found to be secreted in the culture filtrate. This peptide inhibitor was however ineffective on the other enzymes.
Sharma
A
A
Food Technology & Enzyme Engineering Division, Bhabha Atomic Research Centre, Bombay, India.
Padwal-Desai
S R
SR
Ninjoor
V
V
D001230:Aspergillus / Q000201:enzymology*; D001231:Aspergillus flavus / Q000201:enzymology*; D010450:Endopeptidases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007930:Leucine / Q000031:analogs & derivatives; D009943:Organophosphorus Compounds; D010618:Phenanthrolines; D011480:Protease Inhibitors; D011691:Puromycin; D012697:Serine Endopeptidases; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity; D013696:Temperature
D009943:Organophosphorus Compounds; D010618:Phenanthrolines; D011480:Protease Inhibitors; D011691:Puromycin; D010450:Endopeptidases; D012697:Serine Endopeptidases; C032923:microbial serine proteinases; D007930:Leucine; C012211:ubenimex; C025205:1,10-phenanthroline; C005073:ethephon