| Autor: |
Ge, Zhongqi, Liu, Guanzhang, Zeng, Bo, Liu, Xin, Zhang, Guangya |
| Zdroj: |
Biomass Conversion & Biorefinery; Jul2024, Vol. 14 Issue 13, p14325-14337, 13p |
| Abstrakt: |
Efficient degradation of biomass polysaccharide into fermentable sugars by enzymes is a hotspot for sustainable production of valuable chemicals and biofuels. However, enzyme preparation, storage, immobilization, and enhancement of its catalytic performance have always been the unresolved challenges. Herein, we propose a scalable and simple "four-in-one" strategy to deal with the challenges with xylanase as the model enzyme and ferritin as the versatile tag. Interestingly, the target xylanases could efficiently self-assemble into insoluble active xylanase aggregates (IAXAs) in the cell, which facilitates the preparation by low-speed centrifugation with high yield (about 2 g/L). The IAXAs with a purity above 90% could be directly used as self-immobilized xylanases without additional immobilization process. They had good storage stability (170% of the residual activity after 20 days at 30℃) and excellent reusability (88% of the original activity after being reused 20 times). More encouragingly, the IAXAs could spontaneously dissolve back into the buffer and form the soluble polymeric xylanases (SPXs), which showed increased specific activity (312%) and catalytic efficiency (106%) compared with the free ones. Besides, the half-life of SPXs was 73 min at 55℃, which was 37 times than that of the free ones. The potentials of SPXs for biomass polysaccharide xylan were also evaluated. These results confirmed that ferritin could be a valuable tag to mediate target enzymes self-assemble in vivo, which may greatly facilitate the preparation of the enzymes and enhance their catalytic properties and definitely has great scientific and economic potentials in biomass treatment as well as biocatalysis. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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