Evidence map›Paper›PMID 40551120›Full record

ArticleMicrobial cell factories2025

Harnessing magnetic cross-linked cell aggregates (CLCAs) for cost-effective preparation of Konjac mannan-oligosaccharide.

Baoyu Cui, Haiqiang Lu, Xue Liu, Yiran Zhang, Xinxi Gu

Abstract read
In one paragraph

Article in Microbial cell factories, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Baoyu CuiCollege of Food Science and Technology, Hebei Agricultural University, Baoding, 071001, China.
Haiqiang LuCollege of Food Science and Technology, Hebei Agricultural University, Baoding, 071001, China.
Xue LiuCollege of Food Science and Technology, Hebei Agricultural University, Baoding, 071001, China.
Yiran ZhangCollege of Food Science and Technology, Hebei Agricultural University, Baoding, 071001, China.
Xinxi GuCollege of Food Science and Technology, Hebei Agricultural University, Baoding, 071001, China. guxinxi@hebau.edu.cn.

Funding

Innovative Research Group Project of the National Natural Science Foundation of China 1901631
6 · The paper itself

Abstract

Konjac mannan oligosaccharides (KMOS) are currently popular in food additives for their health benefits. However, the simple and efficient preparation of KMOS is still a challenge. In this study, A novel gene encoding β-mannanase (CsMan134) from Cellvibrio sp. KY-GH-1 was displayed on the surface of E. coli cells. Subsequently, E.coli cells (3 g/L) expressing the mannanase CsMan134 were immobilized using 8% (w/v) polyvinyl alcohol, 3% (w/v) sodium alginate, and 3.5% (w/v) Fe₃O₄ to construct magnetic cross-linked cell aggregates (mag-CLCAs). The mannanase CsMan134 demonstrated the highest catalytic efficiency towards konjac mannan compared to other mannans. Compared to free enzyme, the mag-CLCAs exhibited enhanced enzymatic activity across a range of temperatures and pH levels. Furthermore, the mag-CLCAs showed improved thermal stability, retaining over 80% of its initial activity after heating at 50 °C for 180 min, whereas the free enzyme retained only 50% of its residual activity. Scanning electron microscopy (SEM) and vibrating sample magnetometry (VSM) analyses indicated that the mag-CLCAs also maintained good operational stability, retaining more than 75% of their initial activity over five cycles. The mag-CLCAs were effective in converting konjac mannan into a substantial amount of oligosaccharides with a degree of polymerization (DP) of 2-4. In conclusion, the mag-CLCAs represent a valuable, efficient, and cost-effective biocatalyst for the production of KMOS for industrial applications.

Indexed as

beta-MannosidaseMannansOligosaccharidesCost-Benefit AnalysisEnzyme StabilityEscherichia coliHydrogen-Ion ConcentrationTemperaturebeta-MannosidaseMannansOligosaccharidesCell surface displayCH134Cross-linked cell aggregatesKMOSMannanase

Identifiers

PMID40551120
PMCPMC12186349

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