Mining Arylsulfatase from Genome-Scale Metabolic Pathways of Pseudoalteromonas sp. SR43-6 and Its Agar-Based Desulfurization Applications

Arylsulfatase catalyzes the cleavage of sulfate ester bonds and plays a role in agar desulfation, thereby enhancing agar gel strength and quality. While studying the desulfurization pathway in <i>Pseudoalteromonas</i>sp. SR43-6, a sequence encoding a potential arylsulfatase-<i>Pseudoalteromonas</i> Ars (<i>Ps</i>-Ars)-was found. The enzyme, with <i>p</i>-nitrophenyl sulfate as a substrate, exhibited optimal activity at 35 °C and pH 8.0. Its relative activity (206 U/mg) exceeded that of the recently identified arylsulfatases. Four hundred units of the enzyme removed 86.4% of sulfate groups from <i>Gelidium amansii</i> agar in 4 h, whereas 800 U of the enzyme removed 71.3% of sulfate groups from <i>Gracilaria lemaneiformis</i> agar in 8 h. After enzymatic treatment, <i>G. amansii</i> agar gel strength was enhanced by 32%, and a similar improvement was observed in <i>G. lemaneiformis</i> agar gel strength. Enzymatic agar desulfurization offers mild, quality-retaining, and environmentally friendly advantages, augmenting industrial application prospects.

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Publication Details

Journal
ACS Omega
Published
2025-04-22
DOI
https://doi.org/10.1021/acsomega.5c01356
Citations
1
Primary Topic
Enzyme Production and Characterization
Type
article
Field-Weighted Citation Impact
1.23

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article

Mining Arylsulfatase from Genome-Scale Metabolic Pathways of Pseudoalteromonas sp. SR43-6 and Its Agar-Based Desulfurization Applications

Songzhi Li, Minxiao Wang, Xiangzhao Mao, Hong Jiang et al.
1 citations
ACS Omega
Enzyme Production and Characterization
1.23
article

Mining Arylsulfatase from Genome-Scale Metabolic Pathways of Pseudoalteromonas sp. SR43-6 and Its Agar-Based Desulfurization Applications

Songzhi Li, Minxiao Wang, Xiangzhao Mao, Hong Jiang, Jiayu Li, Huan Zhang, Jie Li, Yanli Chen, Yang Guo
article en
1 citations

Abstract

Arylsulfatase catalyzes the cleavage of sulfate ester bonds and plays a role in agar desulfation, thereby enhancing agar gel strength and quality. While studying the desulfurization pathway in <i>Pseudoalteromonas</i>sp. SR43-6, a sequence encoding a potential arylsulfatase-<i>Pseudoalteromonas</i> Ars (<i>Ps</i>-Ars)-was found. The enzyme, with <i>p</i>-nitrophenyl sulfate as a substrate, exhibited optimal activity at 35 °C and pH 8.0. Its relative activity (206 U/mg) exceeded that of the recently identified arylsulfatases. Four hundred units of the enzyme removed 86.4% of sulfate groups from <i>Gelidium amansii</i> agar in 4 h, whereas 800 U of the enzyme removed 71.3% of sulfate groups from <i>Gracilaria lemaneiformis</i> agar in 8 h. After enzymatic treatment, <i>G. amansii</i> agar gel strength was enhanced by 32%, and a similar improvement was observed in <i>G. lemaneiformis</i> agar gel strength. Enzymatic agar desulfurization offers mild, quality-retaining, and environmentally friendly advantages, augmenting industrial application prospects.

ACS OmegaVol. 10(17)
Institute of Environmental Engineering (PL), Institute of Oceanology (BG), Qingdao University of Technology (CN), Ocean University of China (CN)
National Natural Science Foundation of China, Natural Science Foundation of Hainan Province, Natural Science Foundation of Shandong Province, Taishan Scholar Foundation of Shandong Province, Major Scientific and Technological Innovation Project of Shandong Province, National Key Research and Development Program of China, Fundamental Research Funds for the Central Universities, Science and Technology Support Plan for Youth Innovation of Colleges and Universities of Shandong Province of China
Openalex Percentile: Top 23%
Enzyme Production and Characterization
1.23
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