Substrate specificities of bacterial polyhydroxyalkanoate depolymerases and lipases: bacterial lipases hydrolyze poly(omega-hydroxyalkanoates)
Article Abstract:
Study of the substrate specificities of various bacterial extracellular lipases and polyhydroxyalkanoate (PHA) depolymerases revealed that most lipases could hydrolyze omega- hydroxyalkanoic acid polyesters whereas none of the PHA depolymerases could hydrolyze triolein. Degradation of PHA by lipases demonstrates the wide diversity of lipase substrates and further supports the commercial use of PHA due to its broader biodegradation profile.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
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Polyhydroxyalkanoate degradation is associated with nucleotide accumulation and enhances stress resistance and survival of Pseudomonas oleovorans in natural water microcosms
Article Abstract:
The polyhydroxyalkanoic acid (PHA) depolymerization-minus mutant of Pseudomonas oleovorans was used to evaluate the availability of PHA on the pathogenic bacteria's survival and stress-agent resistance. PHA degradation was concomitant with a rise in adenosine triphosphate and guanosine tetraphosphate levels; the PHA depolymerization-minus strain showed decreased survival compared to the wild-type strain.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
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Poly(3-hydroxybutyrate) synthesis genes in Azotobacter sp. strain FA8
Article Abstract:
Researchers have isolated the genes responsible for poly(3-hydroxybutyrate) (PHB) synthesis in Azotobacter sp. strain FA8. The genes code for PHB polymerase, beta-ketothiolase and acetoacetyl-coenzyme A reductase. The PHB polymerase can only produce PHB from glucose or octanoate, but not from medium-chain-length hydroxyalkanoates.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
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