@incollection{NolteSchoerken2019, author = {Johannes Nolte and Ulrich Sch{\"o}rken}, title = {Comparative analysis of non-natural acceptor glucosylation with sucrase enzymes of family GH 70}, series = {Book of Proceedings of STEPsCON 2018}, url = {https://nbn-resolving.org/urn:nbn:de:hbz:832-epub4-14070}, year = {2019}, abstract = {Mutan- and alternansucrase were analyzed for their non-natural glucosylation potential with catecholic compounds caffeic acid and nordihydroguaiaretic acid (NDGA) as well as with non-catecolic p-coumaric acid and umbellic acid. Mutansucrase accepted both catecholic substrates and high glucosylation yields of 92 \% with caffeic acid and 81 \% with NDGA were obtained. The enzyme showed a clear regio-preference for the catechol 4-OH, which corresponds to findings from our previous work with Leuconostoc and Weissella derived glucansucrases. The substrate spectrum of the alternansucrase was broader and all substrates were successfully glucosylated with a preference for the catechols. Interestingly alternansucrase possessed a different regio-specificity. With caffeic acid the 3-O-α-D-glucoside was the major product. A similar substrate spectrum and regioselectivity pattern was observed in previous glucansucrase screenings only with glucansucrase from strain Weissella beninensis DSM 22752. Therefore it may be concluded that the W. beninensis enzyme is an alternansucrase type enzyme as well.}, language = {en} }