Purification and characterization of two extracellular polyhydroxyalkanoate depolymerases from Pseudomonas mendocina |
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Authors: | Hailong Mao Husheng Jiang Tingting Su Zhanyong Wang |
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Affiliation: | 1. School of Environmental and Biological Engineering, Liaoning Shihua University, Fushun, 113001, China
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Abstract: | 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 °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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