Surface display system of Bacillus subtilis: A promising approach for improving the stability and applications of cellobiose dehydrogenase.

Autor: Wu Z; School of Life Sciences, Jiangsu University, Jiangsu, Zhenjiang, 212013, China., Li P; School of Life Sciences, Jiangsu University, Jiangsu, Zhenjiang, 212013, China., Chen X; School of Life Sciences, Jiangsu University, Jiangsu, Zhenjiang, 212013, China., Feng Y; School of Life Sciences, Jiangsu University, Jiangsu, Zhenjiang, 212013, China., Ma Y; School of Life Sciences, Jiangsu University, Jiangsu, Zhenjiang, 212013, China., Ni Z; School of Life Sciences, Jiangsu University, Jiangsu, Zhenjiang, 212013, China., Zhu D; School of Life Sciences, Jiangsu University, Jiangsu, Zhenjiang, 212013, China., Chen H; School of Life Sciences, Jiangsu University, Jiangsu, Zhenjiang, 212013, China. Electronic address: hyc@ujs.edu.cn.
Jazyk: angličtina
Zdroj: Protein expression and purification [Protein Expr Purif] 2024 Jun; Vol. 218, pp. 106448. Date of Electronic Publication: 2024 Feb 17.
DOI: 10.1016/j.pep.2024.106448
Abstrakt: Cellobiose dehydrogenase (CDH) plays a crucial role in lignocellulose degradation and bioelectrochemical industries, making it highly in demand. However, the production and purification of CDH through fungal heterologous expression methods is time-consuming, costly, and challenging. In this study, we successfully displayed Pycnoporus sanguineus CDH (psCDH) on the surface of Bacillus subtilis spores for the first time. Enzymatic characterization revealed that spore surface display enhanced the tolerance of psCDH to high temperature (80 °C) and low pH levels (3.5) compared to free psCDH. Furthermore, we found that glycerol, lactic acid, and malic acid promoted the activity of immobilized spore-displayed psCDH; glycerol has a more significant stimulating effect, increasing the activity from 16.86 ± 1.27 U/mL to 46.26 ± 3.25 U/mL. After four reuse cycles, the psCDH immobilized with spores retained 48% of its initial activity, demonstrating a substantial recovery rate. In conclusion, the spore display system, relying on cotG, enables the expression and immobilization of CDH while enhancing its resistance to adverse conditions. This system demonstrates efficient enzyme recovery and reuse. This approach provides a novel method and strategy for the immobilization and stability enhancement of CDH.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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