Enzymatic degradation behavior of comonomer compositionally fractionated bacterial poly(3-hydroxybutyrate -co-3-hydroxyvalerate)s by poly(3-hydroxyalkanoate) depolymerases isolated from Ralstonia pickettii T1 and Acidovorax sp. TP4

• Published in: Polymer degradation and stability Vol. 84; no. 1; pp. 95 - 104
• Main Authors: Feng, Lidan, Wang, Yi, Inagawa, Yasuhide, Kasuya, Kenichi, Saito, Terumi, Doi, Yoshiharu, Inoue, Yoshio
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.04.2004; Elsevier Science
• Subjects: Applied sciences; Biodegradation; Chemical reactions and properties; Copolyester; Degradation; Exact sciences and technology; Organic polymers; PHA depolymerases; Physicochemistry of polymers; Poly(hydroxyalkanoate); Biodegradation; Poly(hydroxyalkanoate); Copolyester; PHA depolymerases; Biological properties; Valerate(hydroxy) copolymer; Property composition relationship; Biodegradability; Ralstonia pickettii; Butyrate(hydroxy) copolymer; Experimental study; Hydrolysis; Ester copolymer; Poly(hydroxyalkanoat); Enzymatic digestion; Reaction mechanism; Bacteria
• ISSN: 0141-3910; 1873-2321
• DOI: 10.1016/j.polymdegradstab.2003.09.016

The enzymatic hydrolysis behavior of compositionally well-fractionated bacterial poly(3-hydroxybutyrate- co-3-hydroxyvalerate) [P(3HB- co-3HV)] with 3HV-unit content from 8 to 98 mol% and bacterial poly(3-hydroxybutyrate) [P(3HB)] has been investigated in the presence of poly(3-hydroxyalkanoate) depolymerases isolated from Ralstonia pickettii T1 and Acidovorax sp. TP4. The water-soluble degradation products were characterized by HPLC and 1H NMR spectroscopy. P(3HB- co-3HV)s with the whole range of 3HV-unit content can be degraded by R. pickettii T1 depolymerase, while only P(3HB- co-3HV)s with 3HV-unit content less than 80 mol% can be degraded by Acidovorax sp. TP4 depolymerase. It was found that the enzymatic degradation behavior of fractionated P(3HB- co-3HV)s was affected not only by the comonomer unit composition and its distribution but also by the solid-state structure of P(3HB- co-3HV)s and further by the bacterial source of depolymerases. Based on the results, the mechanism of enzymatic degradation was discussed.