Structure of branching enzyme- and amylomaltase modified starch produced from well-defined amylose to amylopectin substrates

Waraporn Sorndech; Domenico Sagnelli; Sebastian Meier; Anita M. Jansson; Byung-Hoo Lee; Bruce R. Hamaker; Agnès Rolland-Sabaté; Kim H. Hebelstrup; Sunanta Tongta; Andreas Blennow

doi:10.1016/j.carbpol.2016.06.097

Structure of branching enzyme- and amylomaltase modified starch produced from well-defined amylose to amylopectin substrates

Waraporn Sorndech, Domenico Sagnelli, Sebastian Meier, Anita M. Jansson, Byung-Hoo Lee, Bruce R. Hamaker, Agnès Rolland-Sabaté, Kim H. Hebelstrup, Sunanta Tongta, Andreas Blennow

Planteglycobiologi

22 Citationer (Scopus)

Abstract

Thermostable branching enzyme (BE, EC 2.4.1.18) from Rhodothermus obamensis in combination with amylomaltase (AM, EC 2.4.1.25) from Thermus thermophilus was used to modify starch structure exploring potentials to extensively increase the number of branch points in starch. Amylose is an important constituent in starch and the effect of amylose on enzyme catalysis was investigated using amylose-only barley starch (AO) and waxy maize starch (WX) in well-defined ratios. All products were analysed for amylopectin chain length distribution, α-1,6 glucosidic linkages content, molar mass distribution and digestibility by using rat intestinal α-glucosidases. For each enzyme treatment series, increased AO content resulted in a higher rate of α-1,6 glucosidic linkage formation but as an effect of the very low initial branching of the AO, the final content of α-1,6 glucosidic linkages was slightly lower as compared to the high amylopectin substrates. However, an increase specifically in short chains was produced at high AO levels. The molar mass distribution for the enzyme treated samples was lower as compared with substrate WX and AO, indicating the presence of hydrolytic activity as well as cyclisation of the substrate. For all samples, increased amylose substrate showed decreased α- and β-amylolysis. Surprisingly, hydrolysis with rat intestinal α-glucosidases was higher with increasing α-1,6 glucosidic linkage content and decreasing M¯w indicating that steric hindrance towards the α-glucosidases was directed by the molar mass rather that the branching density of the glucan per se. Our data demonstrate that a higher amylose content in the substrate starch efficiently produces α-1,6 glucosidic linkages and that the present of amylose generates a higher M¯w and more resistant product than amylopectin. The combination of BE→AM→BE provided somewhat more resistant α-glucan products as compared to BE alone.

Originalsprog	Engelsk
Tidsskrift	Carbohydrate Polymers
Vol/bind	152
Sider (fra-til)	51-61
Antal sider	11
ISSN	0144-8617
DOI	https://doi.org/10.1016/j.carbpol.2016.06.097
Status	Udgivet - 5 nov. 2016

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10.1016/j.carbpol.2016.06.097

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title = "Structure of branching enzyme- and amylomaltase modified starch produced from well-defined amylose to amylopectin substrates",

abstract = "Thermostable branching enzyme (BE, EC 2.4.1.18) from Rhodothermus obamensis in combination with amylomaltase (AM, EC 2.4.1.25) from Thermus thermophilus was used to modify starch structure exploring potentials to extensively increase the number of branch points in starch. Amylose is an important constituent in starch and the effect of amylose on enzyme catalysis was investigated using amylose-only barley starch (AO) and waxy maize starch (WX) in well-defined ratios. All products were analysed for amylopectin chain length distribution, α-1,6 glucosidic linkages content, molar mass distribution and digestibility by using rat intestinal α-glucosidases. For each enzyme treatment series, increased AO content resulted in a higher rate of α-1,6 glucosidic linkage formation but as an effect of the very low initial branching of the AO, the final content of α-1,6 glucosidic linkages was slightly lower as compared to the high amylopectin substrates. However, an increase specifically in short chains was produced at high AO levels. The molar mass distribution for the enzyme treated samples was lower as compared with substrate WX and AO, indicating the presence of hydrolytic activity as well as cyclisation of the substrate. For all samples, increased amylose substrate showed decreased α- and β-amylolysis. Surprisingly, hydrolysis with rat intestinal α-glucosidases was higher with increasing α-1,6 glucosidic linkage content and decreasing M¯w indicating that steric hindrance towards the α-glucosidases was directed by the molar mass rather that the branching density of the glucan per se. Our data demonstrate that a higher amylose content in the substrate starch efficiently produces α-1,6 glucosidic linkages and that the present of amylose generates a higher M¯w and more resistant product than amylopectin. The combination of BE→AM→BE provided somewhat more resistant α-glucan products as compared to BE alone.",

keywords = "Journal Article",

author = "Waraporn Sorndech and Domenico Sagnelli and Sebastian Meier and Jansson, {Anita M.} and Byung-Hoo Lee and Hamaker, {Bruce R.} and Agn{\`e}s Rolland-Sabat{\'e} and Hebelstrup, {Kim H.} and Sunanta Tongta and Andreas Blennow",

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T1 - Structure of branching enzyme- and amylomaltase modified starch produced from well-defined amylose to amylopectin substrates

AU - Sorndech, Waraporn

AU - Sagnelli, Domenico

AU - Meier, Sebastian

AU - Jansson, Anita M.

AU - Lee, Byung-Hoo

AU - Hamaker, Bruce R.

AU - Rolland-Sabaté, Agnès

AU - Hebelstrup, Kim H.

AU - Tongta, Sunanta

AU - Blennow, Andreas

PY - 2016/11/5

Y1 - 2016/11/5

N2 - Thermostable branching enzyme (BE, EC 2.4.1.18) from Rhodothermus obamensis in combination with amylomaltase (AM, EC 2.4.1.25) from Thermus thermophilus was used to modify starch structure exploring potentials to extensively increase the number of branch points in starch. Amylose is an important constituent in starch and the effect of amylose on enzyme catalysis was investigated using amylose-only barley starch (AO) and waxy maize starch (WX) in well-defined ratios. All products were analysed for amylopectin chain length distribution, α-1,6 glucosidic linkages content, molar mass distribution and digestibility by using rat intestinal α-glucosidases. For each enzyme treatment series, increased AO content resulted in a higher rate of α-1,6 glucosidic linkage formation but as an effect of the very low initial branching of the AO, the final content of α-1,6 glucosidic linkages was slightly lower as compared to the high amylopectin substrates. However, an increase specifically in short chains was produced at high AO levels. The molar mass distribution for the enzyme treated samples was lower as compared with substrate WX and AO, indicating the presence of hydrolytic activity as well as cyclisation of the substrate. For all samples, increased amylose substrate showed decreased α- and β-amylolysis. Surprisingly, hydrolysis with rat intestinal α-glucosidases was higher with increasing α-1,6 glucosidic linkage content and decreasing M¯w indicating that steric hindrance towards the α-glucosidases was directed by the molar mass rather that the branching density of the glucan per se. Our data demonstrate that a higher amylose content in the substrate starch efficiently produces α-1,6 glucosidic linkages and that the present of amylose generates a higher M¯w and more resistant product than amylopectin. The combination of BE→AM→BE provided somewhat more resistant α-glucan products as compared to BE alone.

AB - Thermostable branching enzyme (BE, EC 2.4.1.18) from Rhodothermus obamensis in combination with amylomaltase (AM, EC 2.4.1.25) from Thermus thermophilus was used to modify starch structure exploring potentials to extensively increase the number of branch points in starch. Amylose is an important constituent in starch and the effect of amylose on enzyme catalysis was investigated using amylose-only barley starch (AO) and waxy maize starch (WX) in well-defined ratios. All products were analysed for amylopectin chain length distribution, α-1,6 glucosidic linkages content, molar mass distribution and digestibility by using rat intestinal α-glucosidases. For each enzyme treatment series, increased AO content resulted in a higher rate of α-1,6 glucosidic linkage formation but as an effect of the very low initial branching of the AO, the final content of α-1,6 glucosidic linkages was slightly lower as compared to the high amylopectin substrates. However, an increase specifically in short chains was produced at high AO levels. The molar mass distribution for the enzyme treated samples was lower as compared with substrate WX and AO, indicating the presence of hydrolytic activity as well as cyclisation of the substrate. For all samples, increased amylose substrate showed decreased α- and β-amylolysis. Surprisingly, hydrolysis with rat intestinal α-glucosidases was higher with increasing α-1,6 glucosidic linkage content and decreasing M¯w indicating that steric hindrance towards the α-glucosidases was directed by the molar mass rather that the branching density of the glucan per se. Our data demonstrate that a higher amylose content in the substrate starch efficiently produces α-1,6 glucosidic linkages and that the present of amylose generates a higher M¯w and more resistant product than amylopectin. The combination of BE→AM→BE provided somewhat more resistant α-glucan products as compared to BE alone.

KW - Journal Article

U2 - 10.1016/j.carbpol.2016.06.097

DO - 10.1016/j.carbpol.2016.06.097

M3 - Journal article

C2 - 27516249

SN - 0144-8617

VL - 152

SP - 51

EP - 61

JO - Carbohydrate Polymers

JF - Carbohydrate Polymers

ER -

Structure of branching enzyme- and amylomaltase modified starch produced from well-defined amylose to amylopectin substrates

Abstract

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