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

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
Van Der Maarel, Marc J E C ; Capron, Isabelle ; Euverink, Gerrit Jan W ; Bos, Herman Th ; Kaper, Thijs ; Binnema, Doede J. ; Steeneken, Peter A M. / A novel thermoreversible gelling product made by enzymatic modification of starch. Starch/Staerke. Vol. 57 2005. pp. 465-472 (Starch/Staerke).
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title = "A novel thermoreversible gelling product made by enzymatic modification of starch",
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.",
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author = "{Van Der Maarel}, {Marc J E C} and Isabelle Capron and Euverink, {Gerrit Jan W} and Bos, {Herman Th} and Thijs Kaper and Binnema, {Doede J.} and Steeneken, {Peter A M}",
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Van Der Maarel, MJEC, Capron, I, Euverink, GJW, Bos, HT, Kaper, T, Binnema, DJ & Steeneken, PAM 2005, A novel thermoreversible gelling product made by enzymatic modification of starch. in Starch/Staerke. vol. 57, Starch/Staerke, vol. 57, pp. 465-472. https://doi.org/10.1002/star.200500409

A novel thermoreversible gelling product made by enzymatic modification of starch. / Van Der Maarel, Marc J E C; Capron, Isabelle; Euverink, Gerrit Jan W; Bos, Herman Th; Kaper, Thijs; Binnema, Doede J.; Steeneken, Peter A M.

Starch/Staerke. Vol. 57 2005. p. 465-472 (Starch/Staerke; Vol. 57).

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

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T1 - A novel thermoreversible gelling product made by enzymatic modification of starch

AU - Van Der Maarel, Marc J E C

AU - Capron, Isabelle

AU - Euverink, Gerrit Jan W

AU - Bos, Herman Th

AU - Kaper, Thijs

AU - Binnema, Doede J.

AU - Steeneken, Peter A M

PY - 2005/10

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N2 - 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.

AB - 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.

KW - potato starch

KW - gelatin

KW - aardappelzetmeel

KW - gelatine

U2 - 10.1002/star.200500409

DO - 10.1002/star.200500409

M3 - Chapter

SN - 00389056 (ISSN)

VL - 57

T3 - Starch/Staerke

SP - 465

EP - 472

BT - Starch/Staerke

ER -

Van Der Maarel MJEC, Capron I, Euverink GJW, Bos HT, Kaper T, Binnema DJ et al. A novel thermoreversible gelling product made by enzymatic modification of starch. In Starch/Staerke. Vol. 57. 2005. p. 465-472. (Starch/Staerke). https://doi.org/10.1002/star.200500409