Exploring polyhydroxyalkanoates biosynthesis using hydrocarbons as carbon source: a comprehensive review.

Environmental pollution caused by petrochemical hydrocarbons (HC) and plastic waste is a pressing global challenge. However, there is a promising solution in the form of bacteria that possess the ability to degrade HC, making them valuable tools for remediating contaminated environments and effluents. Moreover, some of these bacteria offer far-reaching potential beyond bioremediation, as they can also be utilized to produce polyhydroxyalkanoates (PHAs), a common type of bioplastics. The accumulation of PHAs in bacterial cells is facilitated in environments with high C/N or C/P ratio, which are often found in HC-contaminated environments and effluents. Consequently, some HC-degrading bacteria can be employed to simultaneously produce PHAs and conduct biodegradation processes. Although bacterial bioplastic production has been thoroughly studied, production costs are still too high compared to petroleum-derived plastics. This article aims to provide a comprehensive review of recent scientific advancements concerning the capacity of HC-degrading bacteria to produce PHAs. It will delve into the microbial strains involved and the types of bioplastics generated, as well as the primary pathways for HC biodegradation and PHAs production. In essence, we propose the potential utilization of HC-degrading bacteria as a versatile tool to tackle two major environmental challenges: HC pollution and the accumulation of plastic waste. Through a comprehensive analysis of strengths and weaknesses in this aspect, this review aims to pave the way for future research in this area, with the goal of facilitating and promoting investigation in a field where obtaining PHAs from HC remains a costly and challenging process.

Autoproteolytic activation of the haloalkaliphilic archaeon Natronococcus occultus extracellular serine protease.

The haloalkaliphilic archaeon Natronococcus occultus produces an extracellular serine protease in the stationary growth phase and upon starvation. Two proteins immunologically related to the extracellular protease were detected into the cells: P200 and P190. P200 was detected at early stages of growth and its relative amount decreased as the culture reached the stationary growth phase, concomitantly with the appearance of P190 and proteolytic activity, suggesting that P200 may be the precursor of the secreted protease and P190 the mature enzyme. Both proteins were also detected in the culture medium. Conversion of inactive P200 into active P190 was attained in cell-free culture medium from stationary phase but not from exponential phase. This process was prevented in the presence of PMSF and could be attained by addition of purified mature extracellular protease to P200. Altogether these results indicate that activation of Natronococcus occultus extracellular protease may be autoproteolytic and that factor/s present in stationary phase culture medium may be required for this process.

Purification and biochemical characterization of the haloalkaliphilic archaeon Natronococcus occultus extracellular serine protease.

A serine protease was purified from Natronococcus occultus stationary phase culture medium (328-fold, yield 19%) and characterized at the biochemical level. The enzyme has a native molecular mass of 130 kDa, has chymotrypsin-like activity, is stable and active in a broad pH range (5.5-12), is rather thermophilic (optimal activity at 60 degrees C in 1-2 M NaCl) and is dependent on high salt concentrations for activity and stability (1-2 M NaCl or KCl). Polyclonal antibodies were raised against the purified protease. In Western blots, they presented no cross-reactivity with culture medium from other halobacteria nor with commercial proteases except subtilisin. The amino acid sequences of three tryptic peptides obtained from Natronococcus occultus protease did not show significant similarity to other known proteolytic enzymes. This fact, in addition to its high molecular mass suggests that Natronococcus occultus extracellular protease may be a novel enzyme.