Journal
BIOTECHNOLOGY LETTERS
Volume 35, Issue 11, Pages 1919-1924Publisher
SPRINGER
DOI: 10.1007/s10529-013-1288-1
Keywords
Depolymerase; Polyhydroxyalkanoate; Pseudomonas mendocina; Purification
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Funding
- National Natural Science Foundation of China [31100099]
- Science Project of Liaoning Province Education Office [L2011060]
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Two polyhydroxyalkanoate depolymerases, PHAase I and PHAase II, were purified to homogeneity from the culture supernatant of an effective PHA-degrading bacterium, Pseudomonas mendocina DS04-T. The molecular masses of PHAase I and PHAase II were determined by SDS-PAGE as 59.4 and 33.8 kDa, respectively. Their optimum pH values were 8.5 and 8, respectively. Enzymatic activity was optimal at 50 A degrees C. Both purified enzymes could degrade PHB, PHBV, and P(3HB-co-4HB). Addition of Na+ and K+ slightly increased the rate of PHAase II. EDTA significantly inhibited PHAase II but not PHAase I. Mercaptoethanol and H2O2 also inhibited the activities of both enzymes.
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