ArticleBioresources and bioprocessing2023
Characterization of cold-active trehalose synthase from Pseudarthrobacter sp. for trehalose bioproduction.
Article in Bioresources and bioprocessing, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 3 citations in OpenAlex.
- Dietary Trehalose Activates Autophagy Potentially Via MAPK Signaling Pathway to Alleviate Oxidative Stress Induced by Air Exposure Stress in Chinese Mitten Crab (Aquaculture nutrition · 2025Article
- Engineering a high-sugar tolerant strain of Saccharomyces cerevisiae for efficient trehalose production using a cell surface display approach.Bioresources and bioprocessing · 2024Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Trehalose is a functional sugar that has numerous applications in food, cosmetic, and pharmaceutical products. Production of trehalose from maltose via a single-step enzymatic catalysis using trehalose synthase (TreS) is a promising method compared with the conventional two-step process due to its simplicity with lower formation of byproducts. In this study, a cold-active trehalose synthase (PaTreS) from Pseudarthrobacter sp. TBRC 2005 was heterologously expressed and characterized. PaTreS showed the maximum activity at 20 °C and maintained 87% and 59% of its activity at 10 °C and 4 °C, respectively. The enzyme had remarkable stability over a board pH range of 7.0-9.0 with the highest activity at pH 7.0. The activity was enhanced by divalent metal ions (Mg
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