Polyhydroxyalkanoates Production by Mixed Microbial Culture under High Salinity

PTDC/BTA-BTA/30902/2017 UIDP/04378/2020 UIDB/04378/2020 LA/P/0140/2020The fishing industry produces vast amounts of saline organic side streams that require adequate treatment and disposal. The bioconversion of saline resources into value-added products, such as biodegradable polyhydroxyalkanoates (PHAs), has not yet been fully explored. This study investigated PHA production by mixed microbial cultures under 30 gNaCl/L, the highest NaCl concentration reported for the acclimatization of a PHA-accumulating mixed microbial culture (MMC). The operational conditions used during the culture-selection stage resulted in an enriched PHA-accumulating culture dominated by the Rhodobacteraceae family (95.2%) and capable of storing PHAs up to 84.1% wt. (volatile suspended solids (VSS) basis) for the highest organic loading rate (OLR) applied (120 Cmmol/(L.d)). This culture presented a higher preference for the consumption of valeric acid (0.23 ± 0.03 CmolHVal/(CmolX.h)), and the 3HV monomer polymerization (0.33 ± 0.04 CmmolHV/(CmmolX.h) was higher as well. As result, a P(3HB-co-3HV)) with high HV content (63% wt.) was produced in the accumulation tests conducted at higher OLRs and with 30 gNaCl/L. A global volumetric PHA productivity of 0.77 gPHA/(L.h) and a specific PHA productivity of 0.21 gPHA/(gX.h) were achieved. These results suggested the significant potential of the bioconversion of saline resources into value-added products, such as PHAs.publishersversionpublishe

Pilot-scale valorisation of salmon peptone into polyhydroxyalkanoates by mixed microbial cultures under conditions of high ammonia concentration

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Structural and Functional insights into the catalytic mechanism of the Type II NADH:quinone oxidoreductase family

Type II NADH:quinone oxidoreductases (NDH-2s) are membrane proteins involved in respiratory chains. These proteins contribute indirectly to the establishment of the transmembrane difference of electrochemical potential by catalyzing the reduction of quinone by oxidation of NAD(P)H. NDH-2s are widespread enzymes being present in the three domains of life. In this work, we explored the catalytic mechanism of NDH-2 by investigating the common elements of all NDH-2s, based on the rationale that conservation of such elements reflects their structural/functional importance. We observed conserved sequence motifs and structural elements among 1762 NDH-2s. We identified two proton pathways possibly involved in the protonation of the quinone. Our results led us to propose the first catalytic mechanism for NDH-2 family, in which a conserved glutamate residue, E(172) (in NDH-2 from Staphylococcus aureus) plays a key role in proton transfer to the quinone pocket. This catalytic mechanism may also be extended to the other members of the two-Dinucleotide Binding Domains Flavoprotein (tDBDF) superfamily, such as sulfide:quinone oxidoreductases