Characterization of cold-active trehalose synthase from Pseudarthrobacter sp. for trehalose bioproduction

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�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�0爂/L) using PaTreS yielded 71.7�5.5爂/L trehalose with 4.5�.4爂/L glucose as a byproduct within 16爃. 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: [Figure not available: see fulltext.]. ? 2023 State Key Laboratory of Bioreactor Engineering East China University of Science and Technology.