Journal
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
Volume 26, Issue 11, Pages 1845-1854Publisher
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
DOI: 10.4014/jmb.1606.06036
Keywords
Acceptor specificity; amylosucrase (ASase); Deinococcus radiopugnans; in silico molecular docking; quercetin-3-O-rutinoside (rutin); transglycosylation
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Funding
- National Research Foundation of Korea (NRF) - Korean government (MEST) [2014R1A2A2A05002744]
- National Research Foundation of Korea [2014R1A2A2A05002744] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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The transglycosylation activity of amylosucrase (ASase) has received significant attention owing to its use of an inexpensive donor, sucrose, and broad acceptor specificity, including glycone and aglycone compounds. The transglycosylation reaction of recombinant ASase from Deinococcus radiopugnans (DRpAS) was investigated using various phenolic compounds, and quercetin-3-O-rutinoside (rutin) was found to be the most suitable acceptor molecule used by DRpAS. Two amino acid residues in DRpAS variants (DRpAS Q299K and DRpAS Q299R), assumed to be involved in acceptor binding, were constructed by site-directed mutagenesis. Intriguingly, DRpAS Q299K and DRpAS Q299R produced 10-fold and 4-fold higher levels of rutin transglycosylation product than did the wild-type (WT) DRpAS, respectively. According to in silico molecular docking analysis, the lysine residue at position 299 in the mutants enables rutin to more easily position inside the active pocket of the mutant enzyme than in that of the WT, due to conformational changes in loop 4.
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