Production, Purification and Activity of an Extracellular Depolymerase from Aspergillus fumigatus |
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| Authors: | Thomas M Scherer R Clinton Fuller Robert W Lenz Steve Goodwin |
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| Institution: | (1) Department of Polymer Science and Engineering, University of Massachusetts, Amherst, MA 01003, USA;(2) Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA 01003, USA;(3) Department of Microbiology, University of Massachusetts, Amherst, MA 01003, USA |
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| Abstract: | A strain of Aspergillus fumigatus, which was observed to rapidly degrade poly-3-hydroxybutyrate (PHB) in a leaf compost, was found to secrete an extracellular hydrolase when grown on PHB as the sole carbon source. Isolation and characterization of the PHB hydrolase (depolymerase) from this fungus revealed that the enzyme had a molecular weight of 57 kDa, an isoelectric point of 7.2, and a PHB hydrolysis activity maxima which occurred at 70°C and pH 8.0. Affinity labeling experiments suggested that this fungal hydrolase is a type of serine esterase. The cyclic trimers of 3-hydroxybutyrate were found to reversibly inhibit the enzymes. |
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| Keywords: | Depolymerase enzymatic degradation hydrolase PHB hydrolysis |
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