A novel thermoreversible gelling product made by enzymatic modification of starch

Marc J E C Van Der Maarel, Isabelle Capron, Gerrit Jan W Euverink, Herman Th Bos, Thijs Kaper, Doede J. Binnema, Peter A M Steeneken

Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

Abstract

Amylomaltases or D-enzyme (4-α-glucanotransferases; E.C. 2.4.1.25) are carbohydrate-active enzymes that catalyze the transfer of glucan units from one α-glucan to another in a disproportionation reaction. These enzymes are involved in starch metabolism in plants or maltose/glycogen metabolism in many microorganisms. The amylomaltase of the hyperthermophilic bacterium Thermus thermophilus HB8 was overproduced in Escherichia coli, partially purified and used to modify potato starch. The action of amylomaltase caused the disappearance of amylose and the broadening of the side-chain length distribution in amylopectin, which resulted in a product with both shorter and longer side chains than in the parent starch. Amylomaltase-treated potato starch showed thermoreversible gelation at concentrations of 3% (w/v) or more, thus making it comparable to gelatin. Because of its animal origin, gelatin is not accepted by several consumer groups. Therefore, the amylomaltase-treated potato starch might be a good plant-derived substitute for gelatin. ? 2005 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Original languageEnglish
Title of host publicationStarch/Staerke
Pages465-472
Volume57
DOIs
Publication statusPublished - Oct 2005

Publication series

NameStarch/Staerke
Volume57

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Keywords

  • potato starch
  • gelatin

Cite this

Van Der Maarel, M. J. E. C., Capron, I., Euverink, G. J. W., Bos, H. T., Kaper, T., Binnema, D. J., & Steeneken, P. A. M. (2005). A novel thermoreversible gelling product made by enzymatic modification of starch. In Starch/Staerke (Vol. 57, pp. 465-472). (Starch/Staerke; Vol. 57). https://doi.org/10.1002/star.200500409