Site-directed mutagenesis improves the thermostability of a recombinant Picrophilus torridus trehalose synthase and efficiency for the production of trehalose from sweet potato starch

Hsin Hung Chou, Shu Wei Chang, Guan Chiun Lee, Yi Shan Chen, Tzunuan Yeh, Casimir C. Akoh, Jei Fu Shaw

Research output: Contribution to journalArticle

11 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1017-1022
Number of pages6
JournalFood Chemistry
Issue number3
Publication statusPublished - 2010 Apr 1



  • Amylase
  • Maltose
  • Mutation
  • Proline
  • Sweet potato
  • Thermostability
  • Trehalose
  • Trehalose synthase

ASJC Scopus subject areas

  • Analytical Chemistry
  • Food Science

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