Beschreibung:
<jats:p>Fourteen truncated forms of <jats:italic>Leuconostoc mesenteroides</jats:italic> NRRL B512‐F dextransucrase, involving N‐, C‐ or N‐ plus C‐terminal domain truncations were tested for their ability to bind dextrans. The shortest fragment (14 kDa molecular weight) that still exhibited a strong interaction with dextran was localized between amino acids N1397 and A1527 of the C‐terminal domain (GBD‐7) and consists of six YG repeats. With a dissociation constant <jats:italic>K</jats:italic>
<jats:sub>d</jats:sub> of 2.8 × 10<jats:sup>−9</jats:sup>
M, this motif shows a very high affinity for isomaltohexaose and longer dextrans, supporting the proposed role of GBD in polymer formation. The potential application of GBD‐7 as an affinity tag onto cheap resins like Sephacryl<jats:sup>®</jats:sup> S300HR for rapid purification was evaluated and is discussed.</jats:p>