Recycling the recyclers: strategies for the immobilisation of a PET-degrading cutinase

Bioprocess and Biosystems Engineering, Год журнала: 2025, Номер unknown

Опубликована: Фев. 2, 2025

Abstract Enzymatic degradation of polyethylene terephthalate (PET) represents a sustainable approach to reducing plastic waste and protecting fossil resources. The cost efficiency enzymatic PET processes could be substantially improved by reusing the enzymes. However, conventional immobilisation strategies, such as binding porous carriers, are challenging immobilised enzyme can only interact with macromolecular solid substrate limited extent, thus efficiency. To mitigate this challenge, work compared different strategies PET-degrading cutinase ICCG DAQI . Immobilisation approaches included fixation via linkers synthesis cross-linked aggregates porosities, on stimulus-responsive polymers. highest efficiencies were obtained pH-responsive material Kollicoat ® , where 80% initial activity recovered after immobilisation. Degradation textile fibres cutinase-Kollicoat immobilisate was investigated in batch reactions 1 L-scale. In three consecutive reaction cycles, product yield released terephthalic acid exceeded 97% less than 14 h. Even fifth cycle, 78% maximum achieved same time. An advantage process is efficient pH-dependent recovery reaction, which integrates seamlessly into lowering pH hydrolysis. This integration therefore not simplifies downstream processing, but also provides cost-effective resource-efficient solution for both reuse separation degradation, making it promising industrial application.

Язык: Английский

Immobilization of pullulanase from Bacillus licheniformis on magnetic multi-walled carbon nanotubes for maltooligosaccharide production

Research Square (Research Square), Год журнала: 2024, Номер unknown

Опубликована: Сен. 4, 2024

In this study, Fe₃O₄-coated multi-walled carbon nanotubes (MWCNT-Fe₃O₄) or nickel oxide-coated (MWCNT-NiO) were activated with 3-glycidyloxypropyl)trimethoxysilane to create oxirane groups. Pullulanase from Bacillus licheniformis was covalently immobilized on these magnetic MWCNTs obtain magnetically separable pullunase preparations (MWCNT-Fe₃O₄@Pul MWCNT-NiO@Pul) for producing maltooligosaccharides (MOS) pullulan. The highest recovered activity values obtained as 78% and 85% respectively, MWCNT-Fe₃O₄@Pul MWCNT-NiO@Pul after 24 h of immobilization at pH 7.0. optimal temperature found be 5.5 45°C the free pullulanase, whereas corresponding 50°C both pullulanase preparations. thermal stability increased by 6.2- 8.2-fold 50°C. catalytic efficiencies calculated 0.8- 1.1-fold that respectively. After hydrolysis, MOS yields determined 470 490 mg MOS/g pullulan MWCNT-NiO@Pul, remaining activities 86% 10 reuses,

Язык: Английский

Immobilization of pullulanase from Bacillus licheniformis on magnetic multi-walled carbon nanotubes for maltooligosaccharide production

Chemical Papers, Год журнала: 2024, Номер 78(18), С. 9529 - 9542

Опубликована: Окт. 29, 2024

Язык: Английский