Title Purification and Properties of Extracellular Poly(3-hydroxybutyrate) Depolymerase Produced by Penicillium pinophilum
Author Han, Jeen Sun · Son, Young Jong¹ · Chang, Chung Soon · Kim, Mal Nam *
Address Department of biology, College of Natural Science Sangmyung University; ¹Department of Biochemistry, College of Medicine, Inha University
Bibliography Journal of Microbiology, 36(2),67-73, 1998,
Key Words poly(3-hydroxybutyrate), depolymerase, Penicillium pinophilum
Abstract The extracellular poly(3-hydroxybutyrate)(PHB) depolymerase of Penicilliyum pinophilum ATCC 9644 was purified and characterized. When Penicillum sp. was grown in basal salt medium with PHB as a sole carbon source, higher temperature favored fungal mycelial growth (37℃>30℃>25℃), but enzyme production was lower ar 37℃ than at any other temperatures. The PHB depolymerase was purified using Sepharose CL06B and Sephacryl S0100HR column chromatography. The isolated enzyme was found to be composed of a single polypeptide chain with a molecular weight of about 35 kDa. The optimum condition for the enzyme was pH 6.0 and 50℃, Enzyme activity decreased sharply at temperatures above 50℃. The enzyme was found to be stable in the pH range of 2.0~10.0.1mM Fe^2+ reduced the enzyme activity by 55% abd 4 mM Fe^2+ inhibited it almost completely. The PHB depolymerase (10U) degraded 47% of solvent cast PHB film, while commercial lipase (1000U) of Rhizopus arrhizus degraded 10% of the same specimen, over a period of 48 hours.
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