Production of 3,6-anhydro-l-galactose from agarose by agarolytic enzymes of Saccharophagus degradans 2-40

Eun Ju Yun, Min Hye Shin, Jeong Jun Yoon, Yong Jin Kim, In Geol Choi, Kyoung Heon Kim

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

Saccharophagus degradans 2-40 is capable of hydrolyzing agarose, a red macroalgae-derived polymer, into d-galactose and 3,6-anhydro-l-galactose (L-AHG). Its agarase system is receiving much attention because it can be used to produce fermentable sugar from agarose. L-AHG is commercially unavailable and is considered a rare sugar with a high value. In this study, cells grown on agarose, agar or red macroalgae biomass were found to have a significantly higher agarase activity and AHG-generating activity than those grown on glucose or galactose. From agar-grown cells, both the volumetric activities of agarases and AHG generation in the cell-free lysate were much higher than in the extracellular fraction. Based on the analyses of the enzyme reaction products, from the reaction with the crude enzymes from cell-free lysate, neoagarobiose with a degree of polymerization (DP) 2 appeared to be the only major product in the initial reaction period, but sugars with DPs 2, 4 and 6 were found to be all predominantly produced by the extracellular enzymes in the initial reaction period. Quantitative analysis of AHG using gas chromatography-mass spectrometry with a derivatization step was also found to be highly reproducible and reliable. These results will be useful for producing L-AHG as a rare sugar to investigate its metabolic fate and commercial utilization.

Original languageEnglish
Pages (from-to)88-93
Number of pages6
JournalProcess Biochemistry
Volume46
Issue number1
DOIs
Publication statusPublished - 2011 Jan

Keywords

  • 3,6-Anhydro-l-galactose
  • Agarase
  • Gas chromatography-mass spectrometry
  • Red macroalgae
  • Saccharophagus degradans

ASJC Scopus subject areas

  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology

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