ArticlePlant cell reports2025
Production and purification of tag-free recombinant human acid sphingomyelinase in Nicotiana benthamiana.
Article in Plant cell reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Vector minimization and infiltration optimization for enhanced protein expression in Nicotiana benthamiana.Plant cell reports · 2026Article
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Authors and funding
4 authors.
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Abstract
key messageTag-free, functional human acid sphingomyelinase was successfully produced in a plant-based system. Apoplastic wash fluid extraction improved downstream processing, and a two-step ion exchange chromatography enabled purification of plant-derived ASM. Acid sphingomyelinase (ASM) converts sphingomyelin into phosphocholine and ceramide, a process essential for various cellular functions. Given the relevance of ASM to human health and its potential as a therapeutic enzyme, the development of efficient recombinant production systems is of significant interest in biotechnology. We here developed a plant-based expression system for producing human ASM and targeted major limitations related to its purification. The purification was improved in two ways: by engineering a truncated ASM with a plant-derived secretion signal peptide and by utilizing apoplastic wash fluid extraction to improve the purification process. Recombinant ASM was produced in N. benthamiana as a functional protein using an Agrobacterium-mediated transient expression system. The recombinant ASM was then purified using a two-step ion exchange chromatography method, ensuring high purity. After purification, the ASM yield reached approximately 3.5 mg per kg of fresh leaf weight, with a yield of 49.14% and a 21.2-fold purification enhancement. The purified enzyme exhibited a specific activity of 128.18 ± 4.18 mU/mg, confirming that the plant-derived ASM was functionally active. This work represents the first successful production of human ASM in plants, along with the development of an optimized purification method. This achievement marks a significant step forward in overcoming the challenges associated with producing and purifying recombinant proteins in plant-based expression systems, paving the way for future therapeutic applications.
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