N link to NCBI taxonomic web page and E link to ESTHER gene locus found in this strain. > cellular organisms: NE > Bacteria: NE > unclassified Bacteria (miscellaneous): NE > bacterium HR29: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MQVVLGRVRSAGLLAALLALAAWALVWASPSAEAQSNPYQRGPNPTRSAL TTDGPFSVATYSVSRLSVSGFGGGVIYYPTGTTLTFGGIAMSPGYTADAS SLAWLGRRLASHGFVVIVINTNSRLDFPDSRASQLSAALNYLRTSSPSAV RARLDANRLAVAGHSMGGGATLRISEQIPTLKAGVPLTPWHTDKTFNTPV PQLIVGAEADTVAPVSQHAIPFYQNLPSTTPKVYVELDNATHFAPNSPNA AISVYTISWMKLWVDNDTRYRQFLCNVNDPALSDFRSNNRHCQ
Title: Perspectives on the Role of Enzymatic Biocatalysis for the Degradation of Plastic PET Magalhaes RP, Cunha JM, Sousa SF Ref: Int J Mol Sci, 22:11257, 2021 : PubMed
Plastics are highly durable and widely used materials. Current methodologies of plastic degradation, elimination, and recycling are flawed. In recent years, biodegradation (the usage of microorganisms for material recycling) has grown as a valid alternative to previously used methods. The evolution of bioengineering techniques and the discovery of novel microorganisms and enzymes with degradation ability have been key. One of the most produced plastics is PET, a long chain polymer of terephthalic acid (TPA) and ethylene glycol (EG) repeating monomers. Many enzymes with PET degradation activity have been discovered, characterized, and engineered in the last few years. However, classification and integrated knowledge of these enzymes are not trivial. Therefore, in this work we present a summary of currently known PET degrading enzymes, focusing on their structural and activity characteristics, and summarizing engineering efforts to improve activity. Although several high potential enzymes have been discovered, further efforts to improve activity and thermal stability are necessary.
Title: Secretory expression in Bacillus subtilis and biochemical characterization of a highly thermostable polyethylene terephthalate hydrolase from bacterium HR29 Xi X, Ni K, Hao H, Shang Y, Zhao B, Qian Z Ref: Enzyme Microb Technol, 143:109715, 2021 : PubMed
The environmental threat posed by disposal of plastic wastes has drawn extensive attention in recent years wherein polyethylene terephthalate (PET) constitutes one of the major plastic materials in the wastes. Recycling of PET wastes into reusable materials effectively overcomes its accumulation in the environment and can be achieved by mechanical, chemical, and biological processes. In comparison to the other methods, enzymatic treatment utilizing PET hydrolyzing enzymes (PETases) is environmental-friendly which avoids the use of hazardous chemicals. In this study, we report on the secretory expression in Bacillus subtilis a PETase (BhrPETase) from the bacterium HR29, a close homologue of the leaf-branch compost cutinase (LCC) with 94 % sequence identity. The expression titer of BhrPETase reached 0.66 g/L in an engineered chaperone-overexpression Bacillus subtilis strain, and the biochemical characterization of BhrPETase for the first time revealed its high hydrolyzing activity towards amorphous PET in comparison to two reported PET hydrolyzing enzymes LCC and IsPETase, which were expressed under the same expression conditions in Bacillus subtilis in our study. Most intriguingly, purified BhrPETase displayed a melting temperature as high as 101 degreesC. To our knowledge it is the most thermostable bacterial PETase characterized so far. The superior activity and thermostability of BhrPETase rendered it one of the most promising PETases for plastic waste recycling and bioremediation applications in the future.
Enterobacter sp. bacterium HR29 Poly(Ethylene terephthalate) hydrolase Bis(2-hydroxyethyl) terephthalate ester esterase BhrPETase Bomgl monoacylglycerol lipase