Polyhydroxyalkanoates (PHA), of which polyhydroxybutyrate (PHB) is the most abundant, are polymers of bacterial origin used for various applications in the medical, industrial and agricultural fields. In the present study we worked on the selection, evaluation and improvement of the significant variables of the medium for the production of PHB by ATCC 17697. In order to address the selection of the main factors and optimize the culture medium, a complete factorial experimental design based on the coupled response surface methodology, was presented. The model with the best adjustment of the variables turned out to be quadratic in fructose (C), linear in ammonium sulphate (N) and pH, with interaction in pH and phosphate solution (P), where the pH was the most significant (p < 0.0001) while the micro-elements solution could be neglected. Thus, optimum carbon concentration, adequate nitrogen limitation and interaction between initial pH and phosphate solution concentration are important factors to ensure a high production of PHB. The optimal values of the selected variables were C = 20 g/l, N = 1.5 g/l, P = 8.75 g/l and pH 7.5. A maximum PHB production of 4.6 g/l, obtained under these conditions, increased almost 2.5 times. The polymer accumulated in the cytoplasm of ATCC 17697 in the form of granules showed an FTIR spectrum corresponding to that of commercial PHB.
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http://dx.doi.org/10.1016/j.heliyon.2019.e01374 | DOI Listing |
J Basic Microbiol
September 2021
Laboratorio de Biomateriales, Biomecánica y Bioinstrumentación, Instituto de Tecnologías Emergentes y Ciencias Aplicadas (ITECA), UNSAM-CONICET, Escuela de Ciencia y Tecnología, San Martín, Provincia de Buenos Aires, Argentina.
Polyhydroxyalkanoates (PHA) are polymers produced by microorganisms with increasing commercialization potential; Cupriavidus necator has been the model microorganism to research PHA production. Despite many contributions concerning the formation and degradation of PHA granules, as well as the morphological changes in cells, these phenomena have not been univocally explained yet. Thus, this study aims to integrate the microscopic and analytical analysis to characterize changes in bacterial cell/PHA granules morphology, PHA content, and yield coefficients under different cultivation strategies of C.
View Article and Find Full Text PDFHeliyon
January 2021
School of Science and Technology, National University of San Martín (UNSAM), Av. 25 de mayo 1147, B1650HMK, San Martín, Buenos Aires, Argentina.
Poly(3-hydroxybutyrate) (PHB) belongs to the family of polyhydroxyalkanoates, biopolymers used for agricultural, industrial, or even medical applications. However, scaling up the production is still an issue due to the myriad of parameters involved in the fermentation processes. The present work seeks, firstly, to scale up poly(3-hydroxybutyrate) (PHB) production by wild type ATCC 17697 from shaken flasks to a stirred-tank bioreactor with the optimized media and fructose as carbon source.
View Article and Find Full Text PDFHeliyon
March 2019
UNSAM - National University of San Martín, Av. 25 de mayo 1169, (B1650HMK) San Martín, Buenos Aires, Argentina.
Polyhydroxyalkanoates (PHA), of which polyhydroxybutyrate (PHB) is the most abundant, are polymers of bacterial origin used for various applications in the medical, industrial and agricultural fields. In the present study we worked on the selection, evaluation and improvement of the significant variables of the medium for the production of PHB by ATCC 17697. In order to address the selection of the main factors and optimize the culture medium, a complete factorial experimental design based on the coupled response surface methodology, was presented.
View Article and Find Full Text PDFAlcaligenes eutrophus 335 (ATCC 17697) metabolizes phenol and p-cresol via a catechol meta-cleavage pathway. Studies with mutant strains, each defective in an enzyme of the pathway, showed that the six enzymes assayed are induced by the primary substrate. Studies with a putative polarity mutant defective in the expression of aldehyde dehydrogenase suggested that the structural genes encoding this and subsequent enzymes of the pathway exist in the same operon.
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