Cited by 185biodegradable polymer synthesis and propertiesMicrobial bioremediation and biosurfactantsLipid metabolism and biosynthesis

DEPOLYMERIZATION OF POLY-β-HYDROXYBUTYRATE BY AN INTRACELLULAR ENZYME SYSTEM

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Merrick, J. M., Doudoroff, M.·1964·Journal of Bacteriology

Abstract

Merrick , J. M. (State University of New York, Buffalo), and M. Doudoroff . Depolymerization of poly-β-hydroxybutyrate by an intracellular enzyme system. J. Bacteriol. 88: 60–71. 1964.—The poly-β-hydroxybutyric acid contained in the “lipid granules” of Bacillus megaterium is hydrolyzed to d (−)-β-hydroxybutyric acid by a complex enzyme system present in the soluble enzyme fraction of polymer-depleted cells of Rhodospirillum rubrum . This system consists of a thermostable “activator,” a thermolabile “depolymerase,” and an “esterase.” Under certain conditions, the activator can be replaced by trypsin. Various chemical and physical treatments inactivate the “native lipid granules,” and make them unsuitable as a substrate for the digestive enzymes. This inactivation of the granules is often expressed in the extent rather than the rate of their digestion, and is not correlated with the destruction of the polymer-synthesizing enzymes associated with the granules. The principal product of depolymerase action is d (−)-β-hydroxybutyric acid, but small amounts of esterified products are also released. These are hydrolyzed by the esterase.

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Registry

Crossref · 10.1128/jb.88.1.60-71.1964

Cites

6 of 6 references verified0 citation errors · 0 not checkable

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  • PHB granules isolated from microbial cell extracts could be hydrolyzed to β-hydroxybutyric acid while the polymer was incubated with part of the cell extracts it had been purified from.

    “Merrick, Doudoroff et al. noticed that polyhydroxybutyrate (PHB)”

    From Catalysis as an Enabling Science for Sustainable Polymers (2018) · cites this paper as [469]

  • Depolymerase and esterase could digest inclusion bodies of Bacillus megaterium containing PHB to produce D(-)-β-hydroxybutyric ester, with up to 90% hydrolysis after 100 min.

    “depolymerase”

    From Catalysis as an Enabling Science for Sustainable Polymers (2018) · cites this paper as [469]

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Authors
Merrick, J. M., & Doudoroff, M.
Affiliations
  • University at Buffalo, State University of New York (US)
  • University of California, Berkeley (US)
Venue
Journal of Bacteriology
Published
1964-07
Volume
88
Issue
1
Pages
60-71
ISSN
  • 0021-9193 (ISSN-L)
  • 1098-5530
OpenAlex
W2117373770
Cited by
185
References
6
Citations by year
2026: 1 · 2025: 3 · 2024: 3 · 2023: 4 · 2022: 3 · 2021: 4 · 2020: 6 · 2019: 2 · 2018: 3 · 2017: 4 · 2015: 1 · 2014: 1 · 2013: 4 · 2012: 4
FWCI
4.61
Type
journal article
Language
en
Open access
Locations
  • Journal of Bacteriology (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Physical Sciences › Materials Science › Biomaterials › biodegradable polymer synthesis and properties
  • Physical Sciences › Environmental Science › Pollution › Microbial bioremediation and biosurfactants
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
Keywords
polyhydroxybutyrate, depolymerization, Bacillus megaterium, Rhodospirillum rubrum, lipid granules, depolymerase, esterase, beta-hydroxybutyrate, enzyme activators, trypsin, polyhydroxyalkanoates
MeSH terms
Polyhydroxybutyrates, Bacillus megaterium, Cytoplasmic Granules, Enzymes, Esterases, Hydroxybutyrates, Metabolism, Polyesters, Polymers, Research, Rhodospirillum, Rhodospirillum rubrum, Trypsin

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