4.7 Article

Biodegradation of poly(3-hydroxybutyrate)-derived polymers with different 4-hydroxybutyrate fractions by a novel depolymerase from Paecilomycessp. 1407

Journal

POLYMER DEGRADATION AND STABILITY
Volume 159, Issue -, Pages 107-115

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.polymdegradstab.2018.11.016

Keywords

Poly(3-hydroxybutyrate-co-4-hydroxybutyrate); Paecilomyces sp.; P(3HB-co-4HB) depolymerase; Enzymatic hydrolysis processes; Crystallinity

Funding

  1. National Natural Science Foundation of China [31670122]

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A poly(3-hydroxybutyrate-co-4-hydroxybutyrate) [P(3HB-co-4HB)]-degrading strain was isolated and identified as Paecilomyces sp. A novel P(3HB-co-4HB) depolymerase with a molecular weight of 55 kDa was purified by column chromatography from the culture supernatant of the strain. The purified depolymerase showed optimum activity at pH 6.0 and 30 degrees C, and it was stabilized at pH 4.0-7.0 and below 40 degrees C. The depolymerase degraded poly(3-hydroxybutyrate) (PHB), poly(hydroxybutyrate-co-hydroxyvalerate), and several short-chain-length esters other than P(3HB-co-4HB) but showed no remarkable activity on poly(epsilon-caprolactone) and poly(L-lactic acid). The main enzymatic products comprised hydroxybutyrate monomers, including 3HB and 4HB. The enzymatic erosion rate on the films increased markedly with increasing fraction of 4HB units. Enzymatic hydrolysis processes of PHB and P(3HB-co-4HB) were systematically analyzed in three aspects: enzyme adsorption, single-polymer-chain dissociation, and chemical linkage breakdown. Results indicate that 4HB insertion caused no effect on the degradation of solid-phase PHB-derived material at the molecular chain level but affected enzyme adsorption and crystallinity of the materials. Hindering single-chain stripping by crystallinity dominantly affects the degradation behavior of the polymer. (C) 2018 Published by Elsevier Ltd.

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