Publication list

Publications

11 peer reviewed papers (* marks the most important):   

1) Jensen, J.M., Vester-Christensen, M.B., Møller, M.S., Bønsager, B.C., Christensen, H.E.M., Abou Hachem, M., and Svensson, B. (2011) Efficient secretory expression of functional barley limit dextrinase inhibitor by high cell-density fermentation of Pichia pastoris. Protein Expression Purif., 79, 217–222.

*2) Møller, M.S., Fredslund, F., Majumder, A., Nakai, H., Poulsen, J.-C.N., Lo Leggio, L., Svensson,  B., and Abou Hachem, M. (2012) Enzymology and structure of the GH13_31 glucan 1,6-α-glucosidase that confers isomaltooligosaccharide utilization in the probiotic Lactobacillus acidophilus NCFM. J. Bacteriol., 194, 4249–4259.

*3) Møller, M.S., Abou Hachem, M., Svensson, B., and Henriksen, A. (2012) Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21. Acta Crystallogr.. Sect. F: Struct. Biol. Cryst. Commun., 68, 1008–1012.

4) Abou Hachem, M., Møller, M.S., Andersen, J.M., Fredslund, F., Majumder, A., Nakai, H., Lo Leggio, L., Goh, Y., Barrangou, R., Klaenhammer, T.R., and Svensson, B. (2013) A snapshot into the metabolism of isomalto-oligosaccharides in probiotic bacteria. J. Appl. Glycosci. 60, 95–100.

5) Møller, M.S., Cockburn, D., Nielsen, J.W., Jensen, J.M., Vester-Christensen, M.B., Nielsen, M.M., Andersen, J.M., Wilkens, C., Rannes, J., Hägglund, P., Henriksen, A., Abou Hachem, M., Willemoës, M., and Svensson, B. (2013) Surface Binding Sites (SBSs), mechanism and regulation of enzymes degrading amylopectin and α-limit dextrins. J. Appl. Glycosci. 60, 101–109.

6) Abou Hachem, M., Andersen, J.M., Barrangou, R., Møller, M.S., Fredslund, F., Majumder, A., Ejby, M., Lahtinen, S.J., Jacobsen, S., Lo Leggio, L., Goh, V.J., Klaenhammer, T., and Svensson, B. (2013) Recent insight into oligosaccharide uptake and metabolism in probiotic bacteria. Biocatal. Biotransform. 31, 226–235.

7) Møller, M.S., Goh, Y.J., Viborg, A.H., Andersen, J.M., Klaenhammer, T., Svensson, B., Abou Hachem, M. (2014) Recent insight in α-glucan metabolism in probiotic bacteria. Biologia 69, 713–721.

*8) Møller, M.S., Windahl, M.S., Sim, L., Bøjstrup, M., Abou Hachem, M., Hindsgaul, O., Palcic, M., Svensson, B., and Henriksen, A. (2015) Oligosaccharide and substrate binding in the starch debranching enzyme barley limit dextrinase. J. Mol. Biol. 427, 1263–1277.

*9) Møller, M.S., Vester-Christensen, M.B., Jensen, J.M., Abou Hachem, M., Henriksen, A., and Svensson, B. (2015) Crystal structure of barley limit dextrinase-limit dextrinase inhibitor (LD-LDI) complex reveals insights into mechanism and diversity of cereal-type inhibitors. J. Biol. Chem. 290, 12614–12629.

10) Møller, M.S., Henriksen, A., and Svensson, B. (2016) Structure and function of α-glucan debranching enzymes. Cell. Mol. Life Sci. 73, 2619–2641.

11) Møller, M.S., and Svensson, B. (2016) Structural biology of starch-degrading enzymes and their regulation. Curr. Opin. Struc. Biol. 40, 33–42.

Presentations

Oral talks

“Barley limit dextrinase and its proteinaceous inhibitor – The complex structure”, 6th European Symposium of Enzymes in Grain Processing, Valby, Denmark, November 2011. (Selected from abstract)

“Structure and function of barley limit dextrinase and the complex with its proteinaceous inhibitor”, Nordic Starch Network 2012, Valby, Denmark, November 2012. (Invited)

“The crystal structure of a starch debranching enzyme in complex with a protein inhibitor reveals an extremely tight and novel mode of interaction”, 10th Carbohydrate Bioengineering Meeting, Prague, the Czech Republic, April 2013. (5 min “flash presentation” selected from poster abstract)

“Insights gained from the crystal structure of the complex between barley limit dextrinase and barley limit dextrinase inhibitor”. 5th Symposium on the Alpha-Amylase Family”. Smolenice Castle, Slovakia, October 2013. (Selected from abstract)

“Substrate specificity determinants of barley limit dextrinase”, 23rd CoLuAa meeting (conference for crystallographers from Copenhagen, Lund, and Aarhus), Copenhagen, November 2014. (Selected from abstract)

“New insight into substrate specificity and activity determinants of a starch debranching enzyme gained from substrate:enzyme crystal structures”, 11th Carbohydrate Bioengineering Meeting, Helsinki, Finland, May 2015. (Selected from abstract)

 Poster presentations (International)

“Structure-function relationship investigations and protein engineering of carbohydrate surface binding sites of barley α-amylase 1”, Plant Polysaccharide and Applied Glycoscience Workshop 2010, Tokyo, Japan, July 2010.

“Kinetic analysis of a glycoside hydrolase family 13_31 enzyme from the probiotic bacterium Lactobacillus acidophilus NCFM reveals broad specificity towards isomaltooligosaccharides and polymeric dextran”, 25th International Carbohydrate Symposium, Makuhari (Chiba), Japan, August 2010.

“Isomaltooligosaccharide catabolism in the probiotic bacterium Lactobacillus acidophilus NCFM mediated by 1,6-α-glucosidases from GH13_31”. 4th Symposium on the Alpha-Amylase Family, Smolenice Castle, Slovakia, September 2010.

“Kinetics of barley limit dextrinase hydrolysis of amylopectin and mutational analysis of a putative –3 subsite residue”, 9th Carbohydrate Bioengineering Meeting, Lisbon, Portugal, May 2011.

“A snapshot into the mechanism of an endogenous protein inhibiting a starch α-1,6 debranching enzyme”, Plant and Seaweed Polysaccharides, Nantes, France, July 2012.

“The crystal structure of a starch debranching enzyme in complex with a protein inhibitor reveals an extremely tight and novel mode of interaction”, 10th Carbohydrate Bioengineering Meeting, Prague, the Czech Republic, April 2013. (Including a 5 min “flash presentation” selected from poster abstract)

“Crystal structure of the complex of barley limit dextrinase and its endogenous inhibitor sheds light on a novel cereal-type inhibitor mechanism”, The 27th Annual Symposium of the Protein Society, Boston, USA, July 2013.

“Crystal structure of the complex of barley limit dextrinase and its endogenous inhibitor sheds light on a novel cereal-type inhibitor mechanism”, 5th Symposium on the Alpha-Amylase Family. Smolenice Castle, Slovakia, October 2013. (Awarded 1st poster prize)

”Design of proteinaceous inhibitors of industrially important starch degrading enzymes”, RosettaCON 2014, State of Washington, U.S., July 2014.

“Barley limit dextrinase inhibitor as backbone for design of proteinaceous inhibitors of industrially important enzymes”, RosettaCON 2015, State of Washington, U.S., July 2015

“Barley limit dextrinase inhibitor as backbone for design of proteinaceous inhibitors of industrial starch degrading enzymes”, 67th Mosbacher Kolloquium, Mosbach, Germany, April 2016.