| Autor: |
Srisakul Trakarnpaiboon, Benjarat Bunterngsook, Hataikarn Lekakarn, Daran Prongjit, Verawat Champreda |
| Jazyk: |
angličtina |
| Rok vydání: |
2023 |
| Předmět: |
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| Zdroj: |
Bioresources and Bioprocessing, Vol 10, Iss 1, Pp 1-13 (2023) |
| Druh dokumentu: |
article |
| ISSN: |
2197-4365 |
| DOI: |
10.1186/s40643-023-00681-0 |
| Popis: |
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 (Mg2+, Mn2+ and Ca2+). Conversion of high-concentration maltose syrup (100–300 g/L) using PaTreS yielded 71.7–225.5 g/L trehalose, with 4.5–16.4 g/L glucose as a byproduct within 16 h. The work demonstrated the potential of PaTreS as a promising biocatalyst for the development of low-temperature trehalose production, with the advantages of reduced risk of microbial contamination with low generation of byproduct. Graphical abstract |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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