Conidial and mycelial-bound exo-pectinase of Aspergillus sp.
Intact conidia of Aspergillus sp. were able to degrade pectin 'in vitro' even when protein synthesis was inhibited, thus indicating the presence of cell bound pectinases. At least an exo-pectinase was found and this enzyme was also present in the mycelium of Aspergillus sp. Its presence was not dependent on the carbon source used for growth, suggesting its constitutive nature. This exo-pectinase could be released from conidia or mycelium by incubation at different pH values and the amount of enzyme released could be increased by treatments with chemical agents and hydrolytic enzymes.
Aguilar
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Department of Biotechnology, National University of Mexico, UNAM, D.F.
Huitrón
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D001230:Aspergillus / Q000187:drug effects / Q000201:enzymology*; D003513:Cycloheximide / Q000494:pharmacology; D003902:Detergents / Q000494:pharmacology; D005947:Glucose / Q000378:metabolism; D005990:Glycerol / Q000378:metabolism; D006603:Hexuronic Acids / Q000378:metabolism; D010368:Pectins / Q000378:metabolism; D011096:Polygalacturonase / Q000378:metabolism*; D012995:Solubility; D013172:Spores, Fungal / Q000201:enzymology*; D013213:Starch / Q000378:metabolism
D003902:Detergents; D006603:Hexuronic Acids; C007819:galacturonic acid; D010368:Pectins; D013213:Starch; D003513:Cycloheximide; D011096:Polygalacturonase; D005947:Glucose; D005990:Glycerol