α-Amylase Reagent (Ceralpha)

1.Measurement of α-amylase activity in white wheat flour, milled malt, and microbial enzyme preparations, using the ceralpha assay: Collaborative study. McCleary, B. V., McNally, M., Monaghan, D. & Mugford, D. C. (2002). Journal of AOAC International, 85(5), 1096-1102.
2.Impact of exogenous α-amylases on sugar formation in straight dough wheat bread. Rebholz, G. F., Sebald, K., Dirndorfer, S., Dawid, C., Hofmann, T. & Scherf, K. A. (2020). European Food Research and Technology, 1-12.
3.Heterologous expression of an α-amylase inhibitor from common bean (Phaseolus vulgaris) in Kluyveromyces lactis and Saccharomyces cerevisiae. Brain-Isasi, S., Álvarez-Lueje, A. & Higgins, T. J. V. (2017). Microbial Cell Factories, 16(1), 110.
4.Analysis of Nanobody–Epitope Interactions in Living Cells via Quantitative Protein Transport Assays. Früholz, S. & Pimpl, P. (2017). Plant Protein Secretion, Methods in Molecular Biology, 1662, pp. 171-182, Humana Press, New York, NY.
5.Vacuolar transport in tobacco leaf epidermis cells involves a single route for soluble cargo and multiple routes for membrane cargo. Bottanelli, F., Foresti, O., Hanton, S. & Denecke, J. (2011). The Plant Cell, 23(8), 3007-3025.
6.Impact of formulation and technological factors on the acrylamide content of wheat bread and bread rolls. Claus, A., Mongili, M., Weisz, G., Schieber, A. & Carle, R. (2008). Journal of Cereal Science, 47(3), 546-554.
7.The activity of barley α-amylase on starch granules is enhanced by fusion of a starch binding domain from Aspergillus niger glucoamylase. Juge, N., Nøhr, J., Le Gal-Coëffet, M. F., Kramhøft, B., Furniss, C. S., Planchot, V., Archer, D. B., Willianson, G. & Svensson, B. (2006). Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1764(2), 275-284.
8.Targeting of the plant vacuolar sorting receptor BP80 is dependent on multiple sorting signals in the cytosolic tail. daSilva, L. L. P., Foresti, O. & Denecke, J. (2006). The Plant Cell, 18(6), 1477-1497.
9.Overexpression of the Arabidopsis syntaxin PEP12/SYP21 inhibits transport from the prevacuolar compartment to the lytic vacuole in vivo. Foresti, O., daSilva, L. L. P. & Denecke, J. (2006). The Plant Cell, 18(9), 2275-2293.
10.The effect of carbohydrates on α-amylase activity measurements. Baks, T., Janssen, A. E. & Boom, R. M. (2006). Enzyme and Microbial Technology, 39(1), 114-119.