Billig S

References (5)

Title : Low Carbon Footprint Recycling of Post-Consumer PET Plastic with a Metagenomic Polyester Hydrolase - Sonnendecker_2022_ChemSusChem_15_e202101062
Author(s) : Sonnendecker C , Oeser J , Richter PK , Hille P , Zhao Z , Fischer C , Lippold H , Blazquez-Sanchez P , Engelberger F , Ramirez-Sarmiento CA , Oeser T , Lihanova Y , Frank R , Jahnke HG , Billig S , Abel B , Strater N , Matysik J , Zimmermann W
Ref : ChemSusChem , 15 :e202101062 , 2022
Abstract : Our planet is flooded with plastics and the need for sustainable recycling strategies of polymers has become increasingly urgent. Enzyme-based hydrolysis of post-consumer plastic is an emerging strategy for closed-loop recycling of polyethylene terephthalate (PET). The polyester hydrolase PHL7 isolated from a compost metagenome completely hydrolyzed amorphous PET films, releasing 91 mg of terephthalic acid per hour and mg of enzyme. Degradation rates of the PET film of 6.8 microm h -1 were monitored by vertical scanning interferometry. Structural analysis indicated the importance of leucine at position 210 for the extraordinarily high PET-hydrolyzing activity of PHL7. Within 24 h, 0.6 mg enzyme g PET -1 completely degraded post-consumer thermoform PET packaging in an aqueous buffer at 70 degreesC without any energy-intensive pretreatments. Terephthalic acid recovered from the enzymatic hydrolysate was used to synthesize virgin PET, demonstrating the potential of polyester hydrolases as catalysts in sustainable PET recycling processes with a low carbon footprint.
ESTHER : Sonnendecker_2022_ChemSusChem_15_e202101062
PubMedSearch : Sonnendecker_2022_ChemSusChem_15_e202101062
PubMedID: 34129279
Gene_locus related to this paper: 9firm-PHL7

Title : Enzymes for the biofunctionalization of poly(ethylene terephthalate) - Zimmermann_2011_Adv.Biochem.Eng.Biotechnol_125_97
Author(s) : Zimmermann W , Billig S
Ref : Adv Biochem Eng Biotechnol , 125 :97 , 2011
Abstract : The functionalization of synthetic polymers such as poly(ethylene terephthalate) to improve their hydrophilicity can be achieved biocatalytically using hydrolytic enzymes. A number of cutinases, lipases, and esterases active on polyethylene terephthalate have been identified and characterized. Enzymes from Fusarium solani, Thermomyces insolens, T. lanuginosus, Aspergillus oryzae, Pseudomonas mendocina, and Thermobifida fusca have been studied in detail. Thermostable biocatalysts hydrolyzing poly(ethylene terephthalate) are promising candidates for the further optimization of suitable biofunctionalization processes for textile finishing, technical, and biomedical applications.
ESTHER : Zimmermann_2011_Adv.Biochem.Eng.Biotechnol_125_97
PubMedSearch : Zimmermann_2011_Adv.Biochem.Eng.Biotechnol_125_97
PubMedID: 21076908

Title : High level expression of a hydrophobic poly(ethylene terephthalate)-hydrolyzing carboxylesterase from Thermobifida fusca KW3 in Escherichia coli BL21(DE3) - Oeser_2010_J.Biotechnol_146_100
Author(s) : Oeser T , Wei R , Baumgarten T , Billig S , Follner C , Zimmermann W
Ref : J Biotechnol , 146 :100 , 2010
Abstract : The gram-positive thermophilic actinomycete Thermobifida fusca KW3 secretes a highly hydrophobic carboxylesterase (TfCa) that is able to hydrolyze poly(ethylene terephthalate). TfCa was produced in the Escherichia coli strain BL21(DE3) as a fusion protein consisting of a pelB leader sequence to ensure periplasmic localization of the protein and a His(6) tag for use in its purification. To enhance the recombinant enzyme yield, the tfca gene from T. fusca KW3 was successfully optimized for codon usage in E. coli. In addition, the gene expression induction conditions were optimized and the temperature for cell cultivation was lowered to reduce inclusion body formation. The optimized codons and expression conditions yielded 4500-fold higher TfCa activity than the wild-type strain. Using a pH-controlled bioreactor for cultivation, a TfCa protein concentration of 41.6mg/L was achieved.
ESTHER : Oeser_2010_J.Biotechnol_146_100
PubMedSearch : Oeser_2010_J.Biotechnol_146_100
PubMedID: 20156495
Gene_locus related to this paper: thefu-1831

Title : Hydrolysis of cyclic poly(ethylene terephthalate) trimers by a carboxylesterase from Thermobifida fusca KW3 - Billig_2010_Appl.Microbiol.Biotechnol_87_1753
Author(s) : Billig S , Oeser T , Birkemeyer C , Zimmermann W
Ref : Applied Microbiology & Biotechnology , 87 :1753 , 2010
Abstract : We have identified a carboxylesterase produced in liquid cultures of the thermophilic actinomycete Thermobifida fusca KW3 that were supplemented with poly(ethylene terephthalate) fibers. The enzyme hydrolyzed highly hydrophobic, synthetic cyclic poly(ethylene terephthalate) trimers with an optimal activity at 60 degrees C and a pH of 6. V (max) and K (m) values for the hydrolysis were 9.3 micromol(-1) min(-1) mg(-1) and 0.5 mM, respectively. The esterase showed high specificity towards short and middle chain-length fatty acyl esters of p-nitrophenol. The enzyme retained 37% of its activity after 96 h of incubation at 50 degrees C and a pH of 8. Enzyme inhibition studies and analysis of substitution mutants of the carboxylesterase revealed the typical catalytic mechanism of a serine hydrolase with a catalytic triad composed of serine, glutamic acid, and histidine.
ESTHER : Billig_2010_Appl.Microbiol.Biotechnol_87_1753
PubMedSearch : Billig_2010_Appl.Microbiol.Biotechnol_87_1753
PubMedID: 20467738
Gene_locus related to this paper: thefu-1831

Title : Biochemical characterization of the cutinases from Thermobifida fusca - Chen_2010_J.Mol.Catal.B.Enzym_63_121
Author(s) : Chen S , Su L , Billig S , Zimmermann W , Chen J , Wu J
Ref : J Mol Catal B Enzym , 63 :121 , 2010
Abstract : Thermobifida fusca produces two cutinases which share 93% identity in amino acid sequence. In the present study, we investigated the detailed biochemical properties of T. fusca cutinases for the first time. For a better comparison between bacterial and fungal cutinases, recombinant Fusarium solani pisi cutinase was subjected to the similar analysis. The results showed that both bacterial and fungal cutinases are monomeric proteins in solution. The bacterial cutinases exhibited a broad substrate specificity against plant cutin, synthetic polyesters, insoluble triglycerides, and soluble esters. In addition, the two isoenzymes of T. fusca and the F.solani pisi cutinase are similar in substrate kinetics, the lack of interfacial activation, and metal ion requirements. However, the T.fusca cutinases showed higher stability in the presence of surfactants and organic solvents. Considering the versatile hydrolytic activity, good tolerance to surfactants, superior stability in organic solvents, and thermostability demonstrated by T. fusca cutinases, they may have promising applications in related industries.
ESTHER : Chen_2010_J.Mol.Catal.B.Enzym_63_121
PubMedSearch : Chen_2010_J.Mol.Catal.B.Enzym_63_121
PubMedID:
Gene_locus related to this paper: thefu-q6a0i4 , thefu-q6a0i3