Mining Arylsulfatase from Genome-Scale Metabolic Pathways of Pseudoalteromonas sp. SR43-6 and Its Agar-Based Desulfurization Applications
Year: 2025
Type: article
Abstract: High Resolution Image Download MS PowerPoint Slide 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 Pseudoalteromonas sp. SR43-6, a sequence encoding a potential arylsulfatase─ Pseudoalteromonas Ars ( Ps -Ars)─was found. The enzyme, with p -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 Gelidium amansii agar in 4 h, whereas 800 U of the enzyme removed 71.3% of sulfate groups from Gracilaria lemaneiformis agar in 8 h. After enzymatic treatment, G. amansii agar gel strength was enhanced by 32%, and a similar improvement was observed in G. lemaneiformis agar gel strength. Enzymatic agar desulfurization offers mild, quality-retaining, and environmentally friendly advantages, augmenting industrial application prospects.
Source: ACS Omega
Authors: Songzhi Li, Yang Guo, Hong Jiang, Huan Zhang, Jiayu Li, Yanli Chen, Jie Li, Xiangzhao Mao, Minxiao Wang
Language: English
Subfield: Biotechnology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $1,935
Funders: National Natural Science Foundation of China, Chinese Academy of Sciences, Ocean University of China, Natural Science Foundation of Hainan Province, Natural Science Foundation of Shandong Province, Taishan Scholar Foundation of Shandong Province, Qingdao University, Major Scientific and Technological Innovation Project of Shandong Province, Institute of Oceanology, Chinese Academy of Sciences, 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 ID: W4409683913