This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Merrick, J. M. Articles by Pfister, R. M. Search for Related Content PubMed PubMed Citation Articles by Merrick, J. M. Articles by Pfister, R. M.

 Previous Article  |  Next Article 

J Bacteriol. 1965 January; 89(1): 234-239
Copyright © 1965 American Society for Microbiology. All Rights Reserved.

Morphological Changes in Poly-ß-Hydroxybutyrate Granules Associated with Decreased Susceptibility to Enzymatic Hydrolysis

Department of Biochemistry, School of Medicine, State University of New York at Buffalo, Buffalo, New York
Department of Bacteriology and Botany, Syracuse University, Syracuse, New York

ABSTRACT

MERRICK, J. M. (State University of New York, Buffalo), D. G. LUNDGREN, AND R. M. PFISTER. Morphological changes in poly-ß-hydroxybutyrate granules associated with decreased susceptibility to enzymatic hydrolysis. J. Bacteriol. 89:234–239. 1965.—A complex enzyme system obtained from extracts of Rhodospirillum rubrum cells hydrolyzes poly-ß-hydroxybutyric acid (PHB) contained in native PHB granules isolated from Bacillus megaterium. A labile factor associated with the granules and necessary for depolymerization is easily destroyed by various chemical and physical treatments. Granules inactivated by these treatments were examined in an electron microscope. In all cases, the distinct morphological appearance of native granules was altered. Morphological changes were mainly characterized by membrane fragmentation, loss of coalescence, and surface alterations. These observations suggest that native PHB granules possess definite structural features, disruption of which results in decreased susceptibility of the polymer to enzymatic hydrolysis.

This article has been cited by other articles:

• Uchino, K., Saito, T., Jendrossek, D. (2008). Poly(3-Hydroxybutyrate) (PHB) Depolymerase PhaZa1 Is Involved in Mobilization of Accumulated PHB in Ralstonia eutropha H16. Appl. Environ. Microbiol. 74: 1058-1063 [Abstract] [Full Text]  
• Uchino, K., Saito, T., Gebauer, B., Jendrossek, D. (2007). Isolated Poly(3-Hydroxybutyrate) (PHB) Granules Are Complex Bacterial Organelles Catalyzing Formation of PHB from Acetyl Coenzyme A (CoA) and Degradation of PHB to Acetyl-CoA. J. Bacteriol. 189: 8250-8256 [Abstract] [Full Text]  
• Jendrossek, D., Selchow, O., Hoppert, M. (2007). Poly(3-Hydroxybutyrate) Granules at the Early Stages of Formation Are Localized Close to the Cytoplasmic Membrane in Caryophanon latum. Appl. Environ. Microbiol. 73: 586-593 [Abstract] [Full Text]  
• Gebauer, B., Jendrossek, D. (2006). Assay of Poly(3-Hydroxybutyrate) Depolymerase Activity and Product Determination. Appl. Environ. Microbiol. 72: 6094-6100 [Abstract] [Full Text]  
• Handrick, R., Reinhardt, S., Kimmig, P., Jendrossek, D. (2004). The "Intracellular" Poly(3-Hydroxybutyrate) (PHB) Depolymerase of Rhodospirillum rubrum Is a Periplasm-Located Protein with Specificity for Native PHB and with Structural Similarity to Extracellular PHB Depolymerases. J. Bacteriol. 186: 7243-7253 [Abstract] [Full Text]  
• Handrick, R., Reinhardt, S., Focarete, M. L., Scandola, M., Adamus, G., Kowalczuk, M., Jendrossek, D. (2001). A New Type of Thermoalkalophilic Hydrolase of Paucimonas lemoignei with High Specificity for Amorphous Polyesters of Short Chain-length Hydroxyalkanoic Acids. J. Biol. Chem. 276: 36215-36224 [Abstract] [Full Text]