Simple, fast, and efficient process for producing and purifying trehalulose

Food Chem. 2013 Jun 1;138(2-3):1183-8. doi: 10.1016/j.foodchem.2012.11.115. Epub 2012 Dec 5.

Abstract

A new property of recombinant trehalose synthase (GTase) from Thermus thermophilus HB-8 (ATCC 27634) was found and described in this study. GTase can act on sucrose and catalyze trehalulose formation without isomaltose, isomaltulose, or isomelezitose, releasing small amounts of glucose and fructose as byproducts. Maximum trehalulose yield (approximately 81%) was obtained at an optimum temperature of 65°C and was independent of substrate concentration. A simple, fast, and efficient method of producing and purifying trehalulose is then described. In the first step, GTase catalyzed trehalulose formation using a 20% sucrose substrate. Miscellaneous sugars were then rapidly removed, while trehalulose was completely preserved by Saccharomyces cerevisiae cells. Finally, the cells were separated by centrifugation, and salt ions were removed by an ion-exchange resin, subsequently obtaining a high-purity trehalulose solution. A trehalulose recovery rate of over 95% was achieved using this process. This method has a simple process, fast separation efficiency, and low investment in production equipment, so greatly to improve production efficiency and reduce production costs.

Publication types

  • Evaluation Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Biocatalysis
  • Disaccharides / chemistry
  • Disaccharides / isolation & purification*
  • Glucosyltransferases / chemistry
  • Industrial Microbiology / economics
  • Industrial Microbiology / methods*
  • Saccharomyces cerevisiae / metabolism
  • Sucrose / chemistry
  • Thermus thermophilus / chemistry
  • Thermus thermophilus / enzymology*

Substances

  • Bacterial Proteins
  • Disaccharides
  • Sucrose
  • Glucosyltransferases
  • trehalose synthase
  • trehalulose