A new recombinant Picrophilus torridus TSase (PTTS) has the catalytic ability for the conversion of maltose to trehalose by intramolecular transglucosylation. For industrial applications, the high thermostability of the enzyme would be the most important property for reducing the microbial contamination and lower the production cost. Therefore, in this study, we substituted ten selected proline residues of PTTS which differ from two well-known thermostable TSases. Interestingly, we found that the N503 mutant type, namely N503P-PTTS, showed about 39% higher relative activity than that of the wild type at 65 °C for 120 min. The trehalose yield of mutant N503P-PTTS was 1.3-fold higher than that of the wild type with sweet potato starch as substrate at 50 °C for 4 h. This suggests that the proline site substitution technology used in this study is useful for altering enzyme properties and catalytic efficiency for possible industrial applications.
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