Polylactic acid (PLA)
Polylactic acid is a synthetic polymer based on renewable sources (D-, L-lactic acid). It is a bio-degradable polymer and it is often known as poly(lactic acid) or polylactide (abbreviation PLA). PLA is a thermoplastic polyester . The enzymatic degradation is slow and depends on the type of copolymer, degree of crystallinity and additives. The polymer C(CH3)(OH)HCOOH is synthesized by condensation of lactic acid. PLA is in part used as a replacement for some of the fossil-fuel based synthetic polymers.
While in general it is accepted that the ester bonds within the polymer are attacked by esterases and other serine-like hydrolases, only relatively few enzymes have been biochemically characterized in detail. Tough some enzmes are availabe as commercial products. Mainly bacteria and fungi are known act on the polymer. A selection of known enzymes are listed below:
Please cite the database by referring to: P.C.F. Buchholz, H.L. Zhang, P. Perez-Garcia, L-L. Nover, J. Chow, W. R. Streit, J. Pleiss (2022);Plastics degradation by hydrolytic enzymes: the Plastics-Active Enzymes Database - PAZy, https://doi.org/10.1002/prot.26325
Microbial host/enzyme/gene | EC number | Reference | GenBank/ UniProt | PDB entry | NCBI BLAST |
---|---|---|---|---|---|
Bacteria | |||||
Actinomadura keratinilytica T16-1, serine protease | EC 3.4.- | Sukkhum et al., 2009 | none | ||
Amycolatopsis sp. strain 41, protease | EC 3.4.- | Pranamuda, 2001 | none | ||
Amycolatopsis (Nocardia) orientalis, PLAse I (PLase1) | EC 3.4.- | Fan, 2008 | none | ||
Amycolatopsis (Nocardia) orientalis, PLAse II (PLase2) | EC 3.4.- | Fan, 2008 | B0FLR6, | ABY53108.1 | |
Amycolatopsis (Nocardia) orientalis, PLAse III (PLase3) | EC 3.4.- | Fan, 2008 | B0FY08, | ABY67151.1 | |
Paenibacillus amylolyticus TB13, PLaA | EC 3.1.1.1 | Akutsu-Shigeno, 2003, Teeraphatpornchai, 2003 | Q83VDO | BAC67195.1 | |
Alcaligenes sp. , lipase PL | Hoshino, 2002 | ||||
Comamonas acidovorans TB-35, mainly PUR active esterase | EC 3.1.1.1 | Akutsu, 1998 | BAA76305.1 | BAA76305.1 | |
Alcanivorax borkumensis, ABO2449, esterase | EC 3.1.1.1 | Hajhigasemi, 2016 | Q0VLQ1 | Q0VLQ1 | |
Rhodopseudomonas palustris, RPA1511, esterase | EC 3.1.1.1 | Hajhigasemi, 2016 | Q6N9M9 /RPA1511 | 4PSU | Q6N9M9 / CAE26953.1 |
Lederbergia (Bacillus) lentus, protease, subtilisin, 'Savinase' | EC 3.4.- | Oda, 2000 | P29600 / P29599 | P29600.1 / P29599.1 | |
Lederbergia (Bacillus) subtilis, protease, subitlisin, | EC 3.4.- | Oda, 2000 | |||
Lederbergia (Bacillus) licheniformis, protease, subtiisin, subC | EC 3.4.- | Oda, 2000 | P00780 | P00780.2 | |
Metagenome | |||||
Marine metagenome, esterase, MGS0109 (KC986401) | EC 3.1.1.1 | Tchigvintsev, 2015 | KC986401 | KC986401.1 | |
Marine metagenome, esterase, MGS0010 (KF801579) | EC 3.1.1.1 | Tchigvintsev, 2015 | KF801579 | KF801579.1 | |
Marine metagenome, esterase, MGS0105 (KC986400) | EC 3.1.1.1 | Tchigvintsev, 2015 | KC986400 | KC986400.1 | |
PlaM4, depolymerase | Mayumi, 2008 | AB302136 | BAF57210.1 | ||
PlaM7, depolymerase | Mayumi, 2008 | AB302136 | BAF57212.1 | ||
PlaM9, depolymerase | Mayumi, 2008 | AB302140 | BAF57214.1 | ||
Eukaryota | |||||
Parengyodontium album (Tritirachium album), Proteinase K | EC 3.4.21.64 | Yamashita, 2005 | P06873 | 5KXVA | P06873.2 |
Aspergillus oryzae ATCC42149, cutinase CutL1 | EC:3.1.1.74 | Maeda, 2005, Oda, 2000 | P52956 | P52956.1 | |
Cryptococcus sp. S-2, cutinase | EC:3.1.1.74 | Masaki, 2005 | AB102945.1 | AB102945.1 | |