pla

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/geneEC numberReferenceGenBank/ UniProtPDB entryNCBI BLAST
Bacteria
Actinomadura keratinilytica T16-1, serine proteaseEC 3.4.-Sukkhum et al., 2009none
Amycolatopsis sp. strain 41, proteaseEC 3.4.-Pranamuda, 2001none
Amycolatopsis (Nocardia) orientalis, PLAse I (PLase1)EC 3.4.-Fan, 2008none
Amycolatopsis (Nocardia) orientalis, PLAse II (PLase2)EC 3.4.-Fan, 2008B0FLR6, ABY53108.1
Amycolatopsis (Nocardia) orientalis, PLAse III (PLase3)EC 3.4.-Fan, 2008B0FY08, ABY67151.1
Paenibacillus amylolyticus TB13, PLaAEC 3.1.1.1Akutsu-Shigeno, 2003, Teeraphatpornchai, 2003Q83VDO BAC67195.1
Alcaligenes sp. , lipase PL Hoshino, 2002
Comamonas acidovorans TB-35, mainly PUR active esteraseEC 3.1.1.1Akutsu, 1998BAA76305.1 BAA76305.1
Alcanivorax borkumensis, ABO2449, esteraseEC 3.1.1.1Hajhigasemi, 2016Q0VLQ1 Q0VLQ1
Rhodopseudomonas palustris, RPA1511, esteraseEC 3.1.1.1Hajhigasemi, 2016Q6N9M9 /RPA15114PSUQ6N9M9 / CAE26953.1
Lederbergia (Bacillus) lentus, protease, subtilisin, 'Savinase' EC 3.4.-Oda, 2000P29600 / 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, 2000P00780 P00780.2
Metagenome
Marine metagenome, esterase, MGS0109 (KC986401)EC 3.1.1.1Tchigvintsev, 2015KC986401 KC986401.1
Marine metagenome, esterase, MGS0010 (KF801579)EC 3.1.1.1Tchigvintsev, 2015KF801579 KF801579.1
Marine metagenome, esterase, MGS0105 (KC986400)EC 3.1.1.1Tchigvintsev, 2015KC986400 KC986400.1
PlaM4, depolymerase Mayumi, 2008AB302136 BAF57210.1
PlaM7, depolymerase Mayumi, 2008AB302136 BAF57212.1
PlaM9, depolymerase Mayumi, 2008AB302140 BAF57214.1
Eukaryota
Parengyodontium album (Tritirachium album), Proteinase KEC 3.4.21.64Yamashita, 2005P068735KXVAP06873.2
Aspergillus oryzae ATCC42149, cutinase CutL1EC:3.1.1.74Maeda, 2005, Oda, 2000P52956 P52956.1
Cryptococcus sp. S-2, cutinaseEC:3.1.1.74Masaki, 2005AB102945.1 AB102945.1


  • pla.txt
  • Last modified: 2022/03/17 15:01
  • by Golo Feuerriegel