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A Novel PHB Depolymerase from a Thermophilic Streptomyces Sp.

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Abstract

A novel PHB depolymerase from a thermophilic Streptomyces sp. MG was purified to homogeneity by hydrophobic interaction chromatography and gel filtration. The molecular mass of the purified enzyme was 43 kDa as determined by size exclusion chromatography and 41 kDa by SDS-PAGE. The optimum pH and temperature were 8.5 and 60 °C respectively. The enzyme was stable at 50 °C and from pH 6.5–8.5. The enzyme hydrolyzed not only bacterial polyesters, i.e. poly(3-hydroxybutyric acid and poly(3-hydroxybutyrate-co-3-hydroxyvalerate), but also synthetic, aliphatic polyesters such as polypropiolactone, poly(ethylene adipate) and poly(ethylene succinate).

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Authors and Affiliations

  1. National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central 6, 1-1-1 Higashi, 305-8566, Tsukuba, Ibaraki, Japan

    Buenaventurada P. Calabia & Yutaka Tokiwa

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  1. Buenaventurada P. Calabia
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  2. Yutaka Tokiwa
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Correspondence to Yutaka Tokiwa.

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Revisions requested 9 November 2005; Revisions received 12 December 2005

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Calabia, B.P., Tokiwa, Y. A Novel PHB Depolymerase from a Thermophilic Streptomyces Sp.. Biotechnol Lett 28, 383–388 (2006). https://doi.org/10.1007/s10529-005-6063-5

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  • DOI: https://doi.org/10.1007/s10529-005-6063-5

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