Improvement of Soluble Expression, Stability, and Activity of Acetaldehyde Lyase by Elastin-like Polypeptides Fusion for Acetoin Production from Acetaldehyde

Lin, Hui; Zhang, Jiming; Hu, Jie; Ma, Lu; Lai, Kaili; Zheng, Chaosong; Yang, Qiuhua; Zhang, Liaoyuan

doi:10.3390/biom15091216

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Improvement of Soluble Expression, Stability, and Activity of Acetaldehyde Lyase by Elastin-like Polypeptides Fusion for Acetoin Production from Acetaldehyde

by

Hui Lin

^1,2,†,

Jiming Zhang

^1,2,†,

Jie Hu

^1,2,

Lu Ma

^1,2,

Kaili Lai

³,

Chaosong Zheng

^1,2,

Qiuhua Yang

^4,* and

Liaoyuan Zhang

^1,2,*

¹

Institute of Edible Fungi, Fujian Academy of Agricultural Sciences, Fuzhou 350002, China

²

College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou 350002, China

³

College of Food Science, Fujian Agriculture and Forestry University, Fuzhou 350002, China

⁴

Fisheries Research Institute of Fujian, Xiamen 361013, China

^*

Authors to whom correspondence should be addressed.

^†

These authors contribute equally to this work.

Biomolecules 2025, 15(9), 1216; https://doi.org/10.3390/biom15091216

Submission received: 16 July 2025 / Revised: 17 August 2025 / Accepted: 19 August 2025 / Published: 22 August 2025

(This article belongs to the Special Issue Industrial Microorganisms and Enzyme Technologies)

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Abstract

To achieve the large-scale, low-cost preparation of acetaldehyde lyase (ALS), elastin-like polypeptides (ELPs) as non-chromatographic purification tags were employed to develop an ELP-ALS fusion protein in Escherichia coli. Induction expression results demonstrated that the ELPs tag efficiently improved the soluble expression of the ALS enzyme. Through two rounds of inverse transition cycling (ITC), highly pure ELP-ALS was obtained with an enzyme recovery rate of 85.77%, outperforming Ni²⁺-affinity chromatography (66.80%). The comparative analysis of enzymatic properties revealed that ELP fusion markedly improved the stability and substrate tolerance of the ALS enzyme. Kinetic parameter analysis under identical conditions showed that ELP-ALS possessed a V_max of 15.25 U/mg and a k_cat/K_m of 73.05 s⁻¹·M⁻¹, representing 1.86-fold and 2.97-fold improvements over His-ALS, respectively. Fed-batch reaction using ELP-ALS and acetaldehyde as biocatalyst and substrate, respectively, yielded 95.92 g/L acetoin with 49.32% increase compared to His-ALS (64.24 g/L). These results demonstrated the application potential of ELP-ALS as a promising biocatalyst for acetoin production from acetaldehyde due to its lower preparation cost, higher biocatalytic efficiency, better stability, and substrate tolerance.

Keywords: elastin-like polypeptides; acetaldehyde lyase; non-chromatographic purification; stability and substrate tolerance; acetoin production

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MDPI and ACS Style

Lin, H.; Zhang, J.; Hu, J.; Ma, L.; Lai, K.; Zheng, C.; Yang, Q.; Zhang, L. Improvement of Soluble Expression, Stability, and Activity of Acetaldehyde Lyase by Elastin-like Polypeptides Fusion for Acetoin Production from Acetaldehyde. Biomolecules 2025, 15, 1216. https://doi.org/10.3390/biom15091216

AMA Style

Lin H, Zhang J, Hu J, Ma L, Lai K, Zheng C, Yang Q, Zhang L. Improvement of Soluble Expression, Stability, and Activity of Acetaldehyde Lyase by Elastin-like Polypeptides Fusion for Acetoin Production from Acetaldehyde. Biomolecules. 2025; 15(9):1216. https://doi.org/10.3390/biom15091216

Chicago/Turabian Style

Lin, Hui, Jiming Zhang, Jie Hu, Lu Ma, Kaili Lai, Chaosong Zheng, Qiuhua Yang, and Liaoyuan Zhang. 2025. "Improvement of Soluble Expression, Stability, and Activity of Acetaldehyde Lyase by Elastin-like Polypeptides Fusion for Acetoin Production from Acetaldehyde" Biomolecules 15, no. 9: 1216. https://doi.org/10.3390/biom15091216

APA Style

Lin, H., Zhang, J., Hu, J., Ma, L., Lai, K., Zheng, C., Yang, Q., & Zhang, L. (2025). Improvement of Soluble Expression, Stability, and Activity of Acetaldehyde Lyase by Elastin-like Polypeptides Fusion for Acetoin Production from Acetaldehyde. Biomolecules, 15(9), 1216. https://doi.org/10.3390/biom15091216

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Improvement of Soluble Expression, Stability, and Activity of Acetaldehyde Lyase by Elastin-like Polypeptides Fusion for Acetoin Production from Acetaldehyde

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