A poly(butylene succinate) (PBS)-degrading Aspergillus sp. XH0501-a was obtained by ultraviolet light compound LiCl mutagenesis from the Aspergillus sp. XH0501 which was isolated from soil. The enzymatic activity of strain XH0501-a was 38.89% higher than that of the wild-type strain. A novel extracellular PBS-degrading enzyme with a molecular weight of 44.7 kDa was purified to homogeneity from the culture supernatant of XH0501-a strain. The optimum temperature and pH for the enzyme activity was 40°C and pH 8.6, respectively. It was found that Fe2+ and Ca2+ enhanced the enzyme activity, whereas Cu2+ and Hg2+ inhibited it. The primary products after enzymatic degradation were identified by mass spectrometric analysis and the results indicated that the enzyme was of the exo-type and cut the chain from the carboxyl end; the affinity for the substrate was relative to the chain length of the carboxylic ester.
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This work was supported by the National Natural Science Foundation of China (J0830627-2), the Development Program of Jilin Province (20090594) and the Fundamental Research Funds for the Central Universities (09QNJJ019).
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Li, F., Hu, X., Guo, Z. et al. Purification and characterization of a novel poly(butylene succinate)-degrading enzyme from Aspergillus sp. XH0501-a. World J Microbiol Biotechnol 27, 2591–2596 (2011). https://doi.org/10.1007/s11274-011-0731-5
- Poly(butylene succinate)
- Aspergillus sp. XH0501-a
- PBS-degrading enzyme