PLA from PolySciTech used in testing of enzymatic degradation and potential application towards environmental cleanup of plastics

In addition to biomedical applications, polyesters are also applied for environmental considerations as the ester bonds in their backbone can be cleaved by water. In this case, polylactide and other polyesters can be used to further understand various degradation mechanisms which happen environmentally. Researchers from Consejo Superior de Investigaciones Científicas, Barcelona Supercomputing Center, Universidad de Oviedo, Bangor University, and Institució Catalana de Recerca i Estudis Avan?ats used PLA (Cat# AP224) from PolySciTech Division of Akina, Inc. (www.polyscitech.com) to study breakdown of esters under acidic conditions. Read more: Vidal, Paula, Mónica Martínez-Martínez, Laura Fernandez-Lopez, Sergi Roda, Celia Méndez-García, Olga V. Golyshina, Víctor Guallar, Ana I. Peláez, and Manuel Ferrer. "Metagenomic mining for esterases in the microbial community of Los Rueldos acid mine drainage formation." Frontiers in Microbiology 13 (2022). https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9162777/

“Acid mine drainage (AMD) systems are extremely acidic and are metal-rich formations inhabited by relatively low-complexity communities of acidophiles whose enzymes remain mostly uncharacterized. Indeed, enzymes from only a few AMD sites have been studied. The low number of available cultured representatives and genome sequences of acidophiles inhabiting AMDs makes it difficult to assess the potential of these environments for enzyme bioprospecting. In this study, using na?ve and in silico metagenomic approaches, we retrieved 16 esterases from the α/β-hydrolase fold superfamily with the closest match from uncultured acidophilic Acidobacteria, Actinobacteria (Acidithrix, Acidimicrobium, and Ferrimicrobium), Acidiphilium, and other Proteobacteria inhabiting the Los Rueldos site, which is a unique AMD formation in northwestern Spain with a pH of ～2. Within this set, only two polypeptides showed high homology (99.4%), while for the rest, the pairwise identities ranged between 4 and 44.9%, suggesting that the diversity of active polypeptides was dominated not by a particular type of protein or highly similar clusters of proteins, but by diverse non-redundant sequences. The enzymes exhibited amino acid sequence identities ranging from 39 to 99% relative to homologous proteins in public databases, including those from other AMDs, thus indicating the potential novelty of proteins associated with a specialized acidophilic community. Ten of the 16 hydrolases were successfully expressed in Escherichia coli. The pH for optimal activity ranged from 7.0 to 9.0, with the enzymes retaining 33–68% of their activities at pH 5.5, which was consistent with the relative frequencies of acid residues (from 54 to 67%). The enzymes were the most active at 30–65°C, retaining 20–61% of their activity under the thermal conditions characterizing Los Rueldos (13.8 ± 0.6°C). The analysis of the substrate specificity revealed the capacity of six hydrolases to efficiently degrade (up to 1,652 ± 75 U/g at pH 8.0 and 30°C) acrylic- and terephthalic-like [including bis(2-hydroxyethyl)-terephthalate, BHET] esters, and these enzymes could potentially be of use for developing plastic degradation strategies yet to be explored. Our assessment uncovers the novelty and potential biotechnological interest of enzymes present in the microbial populations that inhibit the Los Rueldos AMD system. Keywords: acidophiles, acidophilic bacteria, acid mine drainage, biodiversity, extremozymes, esterase, metagenomics, plastic”