TAILIEUCHUNG - Báo cáo khoa học: Hybrid reuteransucrase enzymes reveal regions important for glucosidic linkage specificity and the transglucosylation / hydrolysis ratio

The reuteransucrase enzymes ofLactobacillus reuteristrain 121 (GTFA) andL. reuteristrain ATCC 55730 (GTFO) convert sucrose into a-d-glu-cans (labelled reuterans) with mainlya-(1fi4) glucosidic linkages (50% and 70%, respectively), plusa-(1fi6) linkages. In the present study, we report a detailed analysis of various hybrid GTFA⁄O enzymes, resulting in the iden- | Hybrid reuteransucrase enzymes reveal regions important for glucosidic linkage specificity and the transglucosylation hydrolysis ratio Slavko Kralj1 2 Sander S. van Leeuwen3 Vincent Valk1 2 Wieger Eeuwema1 2 Johannis P. Kamerling3 and Lubbert Dijkhuizen1 2 1 Centre for Carbohydrate Bioprocessing TNO-University of Groningen Haren The Netherlands 2 Department of Microbiology Groningen Biomolecular Sciences and Biotechnology Institute University of Groningen Haren The Netherlands 3 Department of Bio-Organic Chemistry Bijvoet Center Utrecht University The Netherlands Keywords glucansucrase glycosidic linkage hybrid enzymes product specificity reuteransucrase Correspondence L. Dijkhuizen Department of Microbiology University of Groningen Kerklaan 30 9751 NN Haren The Netherlands Fax 31 50 3632154 Tel 31 50 3632150 E-mail Present address Genencor-A Danisco Division Leiden The Netherlands Received 21 July 2008 revised 2 October 2008 accepted 6 October 2008 doi The reuteransucrase enzymes of Lactobacillus reuteri strain 121 GTFA and L. reuteri strain ATCC 55730 GTFO convert sucrose into a-D-glu-cans labelled reuterans with mainly a- 1fi4 glucosidic linkages 50 and 70 respectively plus a- 1fi6 linkages. In the present study we report a detailed analysis of various hybrid GTFA O enzymes resulting in the identification of specific regions in the N-termini of the catalytic domains of these proteins as the main determinants of glucosidic linkage specificity. These regions were divided into three equal parts A1-3 O1-3 and used to construct six additional GTFA O hybrids. All hybrid enzymes were able to synthesize a-glucans from sucrose and oligosaccharides from sucrose plus maltose or isomaltose as acceptor substrates. Interestingly not only the A2 O2 regions with the three catalytic residues affect glucosidic linkage specificity but also the upstream A1 O1 regions make a strong contribution. Some GTFO derived hybrid mutant .

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