Litcius/Paper detail

<i>Halomonas alkaliantarctica</i> as a platform for poly(3‐hydroxybutyrate‐ <i>co</i> ‐3‐hydroxyvalerate) production from biodiesel‐derived glycerol

Justyna Możejko‐Ciesielska, Krzysztof Moraczewski, Sylwester Czaplicki

2023Environmental Microbiology Reports12 citationsDOIOpen Access PDF

Abstract

Polyhydroxyalkanoates (PHAs) are biodegradable polyesters produced by a wide range of microorganisms, including extremophiles. These unique microorganisms have gained interest in PHA production due to their ability to utilise low-cost carbon sources under extreme conditions. In this study, Halomonas alkaliantarctica was examined with regards to its potential to produce PHAs using crude glycerol from biodiesel industry as the only carbon source. We found that cell dry mass concentration was not dependent on the applying substrate concentration. Furthermore, our data confirmed that the analysed halophile was capable of metabolising crude glycerol into poly(3-hydroxybutyrate-co-3-hydroxyvalerate) copolymer within 24 h of the cultivation without addition of any precursors. Moreover, crude glycerol concentration affects the repeat units content in the purified PHAs copolymers and their thermal properties. Nevertheless, a differential scanning calorimetric and thermogravimetric analysis showed that the analysed biopolyesters have properties suitable for various applications. Overall, this study described a promising approach for the valorisation of crude glycerol as a future strategy of industrial waste management to produce high value microbial biopolymers.

Topics & Concepts

PolyhydroxyalkanoatesHalomonasGlycerolValorisationBiodieselBiodiesel productionThermogravimetric analysisHalophileChemistryMicroorganismPulp and paper industryBiodegradationBiodegradable plasticPolyesterTributyrinFood scienceEnvironmentally friendlyMaterials scienceOrganic chemistryLipaseWaste managementBacteriaBiologyCatalysisEcologyEngineeringGeneticsEnzymebiodegradable polymer synthesis and propertiesCarbon dioxide utilization in catalysisEnzyme Catalysis and Immobilization