A novel PHB depolymerase from a thermophilic Streptomyces sp

Biotechnology Letters
Buenaventurada P Calabia, Yutaka Tokiwa

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 degrees C respectively. The enzyme was stable at 50 degrees 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).

References

May 1, 1982·European Journal of Biochemistry·T TanioS Masamune
Mar 10, 2004·Biotechnology Letters·Buenaventurada P Calabia, Yutaka Tokiwa
Aug 4, 2004·Biotechnology Letters·Yutaka Tokiwa, Buenaventurada P Calabia
Jun 2, 2005·Biotechnology Letters·Hyun-A LimYutaka Tokiwa

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Citations

Feb 24, 2007·Applied Microbiology and Biotechnology·Dieter Jendrossek
Feb 14, 2009·Applied Microbiology and Biotechnology·Christos P PapaneophytouDimitrios A Kyriakidis
Apr 16, 2010·Applied Microbiology and Biotechnology·Qun RenManfred Zinn
Apr 25, 2013·Environmental Science and Pollution Research International·Swapan Kumar GhoshSumanta Ray
Oct 30, 2009·International Journal of Molecular Sciences·Yutaka TokiwaSeiichi Aiba
Jan 15, 2018·Environmental Science and Pollution Research International·Temoor AhmedSher Muhammad
Mar 5, 2018·Applied Microbiology and Biotechnology·Jelena SpasicJasmina Nikodinovic-Runic
Aug 7, 2020·Analytical Methods : Advancing Methods and Applications·Maria Angeles Camacho-RuizJorge A Rodríguez
Nov 20, 2019·Biochimica Et Biophysica Acta. Proteins and Proteomics·Aneta K UrbanekMiguel Arroyo

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