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. 2024 Feb 28;29(5):1039.
doi: 10.3390/molecules29051039.

UCST-Type Soluble Immobilized Cellulase: A New Strategy for the Efficient Degradation and Improved Recycling Performance of Wastepaper Cellulose

Zhaohui Chen  1 , Jiacong Wu  1 , Juan Han  2 , Yun Wang  1 , Liang Ni  1
Affiliations

UCST-Type Soluble Immobilized Cellulase: A New Strategy for the Efficient Degradation and Improved Recycling Performance of Wastepaper Cellulose

Zhaohui Chen et al. Molecules. .

Abstract

This paper reports an innovative study that aims to address key issues in the efficient recycling of wastepaper cellulose. The research team utilized the temperature-responsive upper critical solution temperature (UCST) polymer P(NAGA-b-DMA) in combination with the LytA label's affinity for choline analogs. This innovative approach enabled them to successfully develop a novel soluble immobilized enzyme, P(NAGA-b-DMA)-cellulase. This new enzyme has proven highly effective, significantly enhancing the degradation of wastepaper cellulose while demonstrating exceptional stability. Compared with the traditional insoluble immobilized cellulase, the enzyme showed a significant improvement in the pH, temperature stability, recycling ability, and storage stability. A kinetic parameter calculation showed that the enzymatic effectiveness of the soluble immobilized enzyme was much better than that of the traditional insoluble immobilized cellulase. After the immobilization reaction, the Michaelis constant of the immobilized enzyme was only increased by 11.5%. In the actual wastepaper degradation experiment, the immobilized enzyme was effectively used, and it was found that the degradation efficiency of wastepaper cellulose reached 80% of that observed in laboratory conditions. This novel, thermosensitive soluble immobilized cellulase can efficiently catalyze the conversion of wastepaper cellulose into glucose under suitable conditions, so as to further ferment into environmentally friendly biofuel ethanol, which provides a solution to solve the shortage of raw materials and environmental protection problems in the paper products industry.

Keywords: UCST; catalyze; cellulase; immobilized enzyme; waste-paper cellulose.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Synthesis process of P(NAGA-b-DMA)-cellulase. (a) Synthesis process of NAGA. (b) Synthesis process of CTA. (c) Synthesis process of PNAGA. (d) Synthesis process of P(NAGA-b-DMA). (e) Synthesis process of P(NAGA-b-DMA)-cellulase.
Figure 2
Figure 2
TEM data of P(NAGA-b-DMA) (a) above the UCST and (b) below the UCST.
Figure 3
Figure 3
Laser confocal data of P(NAGA-b-DMA) (a,b) and P(NAGA-b-DMA)-cellulase (c,d).
Figure 4
Figure 4
SEM data of P(NAGA-b-DMA) (a) and P(NAGA-b-DMA)-cellulase (b).
Figure 5
Figure 5
Effects of enzyme concentration (a) and substrate addition (b) on catalytic performance.
Figure 6
Figure 6
Comparison of catalytic performance between free cellulase and immobilized cellulase.
See this image and copyright information in PMC

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