Enzymatic Synthesis of Glucosyl Rebaudioside A and its Characterization as a Sweetener

J Food Sci. 2019 Nov;84(11):3186-3193. doi: 10.1111/1750-3841.14821. Epub 2019 Oct 7.

Abstract

Rebaudioside A was modified via glucosylation by recombinant dextransucrase of Leuconostoc lactis EG001 in Escherichia coli BL21 (DE3), forming single O-α-D-glucosyl-(1″→6') rebaudioside A with yield of 86%. O-α-D-glucosyl-(1″→6') rebaudioside A was purified using HPLC and Diaion HP-20 and its properties were characterized for possible use as a food ingredient. Almost 98% of O-α-D-glucosyl-(1″→6') rebaudioside A was dissolved after 15 days of storage at room temperature, compared to only 11% for rebaudioside A. Compared to rebaudioside A, O-α-D-glucosyl-(1″→6') rebaudioside A showed similar or improved acidic or thermal stability in commercial drinks. Thus, O-α-D-glucosyl-(1″→6') rebaudioside A could be used as a highly pure and improved sweetener with high stability in commercial drinks. PRACTICAL APPLICATION: The proposed method can be used to generate glucosyl rebaudioside A by enzymatic glucosylation. Simple glucosyl rebaudioside A exhibited high acid/thermal stability and improved sweetener in commercialized drinks. This method can be applied to obtain high value-added bioactive compounds by enzymatic modification.

Keywords: Leuconostoc lactis; Rebaudioside A; glucansucrase; glucosylation; sweetener.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Biocatalysis
  • Chromatography, High Pressure Liquid
  • Diterpenes, Kaurane / chemistry*
  • Glucosyltransferases / chemistry*
  • Leuconostoc / enzymology*
  • Sweetening Agents / chemistry*

Substances

  • Bacterial Proteins
  • Diterpenes, Kaurane
  • Sweetening Agents
  • rebaudioside A
  • Glucosyltransferases
  • dextransucrase