Immobilized cutinases: Preparation, solvent tolerance and thermal stability

Su, An; Shirke, Abhijit N.; Baik, Joshua; Zou, Yi; Gross, Richard A.

doi:10.1016/j.enzmictec.2018.05.010

Cited by 34 publications

(20 citation statements)

References 71 publications

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“…When compared to 44% (Na 2 HPO 4 \NaH 2 PO 4 ) and 19% (K 2 HPO 4 \KH 2 PO 4 ) immobilization yield in the reactions with 1 M buffers, lower salt concentrations of 0.1 M seemed to have a favorable effect on the coupling of CaLB to polypropylene beads. Similar results were obtained when using Tris-HCl and MOPS buffers (see ESI, Figure S1) and are confirmed by literature [37,38]. After 24 h, only 7% of the activity was left in the supernatants (1 M MOPS) while for the others buffer systems almost all enzyme was immobilised.…”

Section: Lipase Immobilizationsupporting

confidence: 89%

“…The integration of the peak at 4.1 ppm compared with the peak of the -CH 2 adjacent to the carbonylic carbon groups of DMA (2.3 ppm) was used to determine the degree of polymerization. results were obtained when using Tris-HCl and MOPS buffers (see ESI, Figure S1) and are confirmed by literature [37,38]. After 24 h, only 7% of the activity was left in the supernatants (1 M MOPS) while for the others buffer systems almost all enzyme was immobilised.…”

Section: Polymerization Of Bio-based Polymerssupporting

confidence: 84%

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Efficient Physisorption of Candida Antarctica Lipase B on Polypropylene Beads and Application for Polyester Synthesis

et al. 2018

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In the present work, Candida antarctica lipase B (CaLB) was adsorbed onto polypropylene beads using different reaction conditions, in order to investigate their influence on the immobilization process and the enzyme activity of the preparations in polymerization reactions. In general, lower salt concentrations were more favorable for the binding of enzyme to the carrier. Polymerisation of dimethyl adipate (DMA) and 1,4-butanediol (BDO) was investigated in thin-film systems at 70 °C and at both atmosphere pressure (1000 mbar) and 70 mbar. Conversion rates and molecular masses of the reaction products were compared with reactions catalyzed by CaLB in its commercially available form, known as Novozym 435 (CaLB immobilized on macroporous acrylic resin). The best results according to molecular weight and monomer conversion after 24 h reaction time were obtained with CaLB immobilized in 0.1 M Na2HPO4\NaH2PO4 buffer at pH 8, producing polyesters with 4 kDa at conversion rates of 96% under low pressure conditions. The stability of this preparation was studied in a simulated continuous polymerization process at 70 °C, 70 mbar for 4 h reaction time. The data of this continuous polymerizations show that the preparation produces lower molecular weights at lower conversion rates, but is comparable to the commercial enzyme concerning stability for 10 cycles. However, after 24 h reaction time, using our optimum preparation, higher molecular weight polyesters (4 kDa versus 3.1 kDa) were obtained when compared to Novozym 435.

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Section: Lipase Immobilizationsupporting

confidence: 89%

Section: Polymerization Of Bio-based Polymerssupporting

confidence: 84%

Efficient Physisorption of Candida Antarctica Lipase B on Polypropylene Beads and Application for Polyester Synthesis

et al. 2018

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“…[14][15][16][17][18][19] Considering the potential for esterases to deconstruct PET under mild conditions, the global research community is vigorously pursuing efforts in prospecting for new PET-degrading enzymes (PET hydrolases), solving crystal structures thereof, and engineering and evolving these enzymes for improved PET degradation capacity, with the aim of developing efficient biocatalysts for use as a chemical recycling approach to address this common polyester. [20][21][22][23][24][25][26][27][28][29][30][31][32][33][34][35][36] Given the growth in research related to biocatalyst development for PET depolymerization, it is critical to understand the projected economic and sustainability impacts that such a process could have toward enabling PET circularity. To that end, we present here a rigorous, comprehensive modeling effort for a conceptual enzymatic process to depolymerize PET to recycled TPA (rTPA) and EG, including all utilities required for an integrated process.…”

Section: Context and Scalementioning

confidence: 99%

Techno-economic, life-cycle, and socioeconomic impact analysis of enzymatic recycling of poly(ethylene terephthalate)

Singh

Rorrer²,

Nicholson³

et al. 2021

Joule

187

252

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This study presents a comprehensive process, economic, environmental, and socioeconomic analysis of the enzymatic recycling of poly(ethylene terephthalate), which is the most widely used synthetic polyester. The analyses predict that PET deconstruction using enzymes can achieve cost parity with terephthalic acid manufacturing as well as substantial reductions in both supply chain energy use and greenhouse gas emissions relative to virgin polyester manufacturing. This study also highlights key research areas for further impactful development of biocatalysis-enabled plastics recycling.

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“…Another Fusarium cutinase adsorbed onto chemically modified gold nanoparticles was used for river and tap water detoxification, with the ability to be reused up to five times [81]. Su et al studied the immobilization of three cutinases from A. oryzae, H. insolens, and T. terrestris through adsorption on a commercial macroporous support (Lewatit VP OC 1600) [82]. The immobilized enzymes showed increased optimal temperatures of 75 • C, and superior thermostability (stable at 70 • C for 1 h) with regard to their free forms.…”

Section: Immobilizationmentioning

confidence: 99%

A Middle-Aged Enzyme Still in Its Prime: Recent Advances in the Field of Cutinases

et al. 2018

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Cutinases are α/β hydrolases, and their role in nature is the degradation of cutin. Such enzymes are usually produced by phytopathogenic microorganisms in order to penetrate their hosts. The first focused studies on cutinases started around 50 years ago. Since then, numerous cutinases have been isolated and characterized, aiming at the elucidation of their structure–function relations. Our deeper understanding of cutinases determines the applications by which they could be utilized; from food processing and detergents, to ester synthesis and polymerizations. However, cutinases are mainly efficient in the degradation of polyesters, a natural function. Therefore, these enzymes have been successfully applied for the biodegradation of plastics, as well as for the delicate superficial hydrolysis of polymeric materials prior to their functionalization. Even though research on this family of enzymes essentially began five decades ago, they are still involved in many reports; novel enzymes are being discovered, and new fields of applications arise, leading to numerous related publications per year. Perhaps the future of cutinases lies in their evolved descendants, such as polyesterases, and particularly PETases. The present article reviews the biochemical and structural characteristics of cutinases and cutinase-like hydrolases, and their applications in the field of bioremediation and biocatalysis.

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Immobilized cutinases: Preparation, solvent tolerance and thermal stability

Cited by 34 publications

References 71 publications

Efficient Physisorption of Candida Antarctica Lipase B on Polypropylene Beads and Application for Polyester Synthesis

Efficient Physisorption of Candida Antarctica Lipase B on Polypropylene Beads and Application for Polyester Synthesis

Techno-economic, life-cycle, and socioeconomic impact analysis of enzymatic recycling of poly(ethylene terephthalate)

A Middle-Aged Enzyme Still in Its Prime: Recent Advances in the Field of Cutinases

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