Amylolytically-resistant tapioca starch modified by combined treatment of branching enzyme and maltogenic amylase
Tapioca starch was modified using branching enzyme (BE) isolated from Bacillus subtilis 168 and Bacillus stearothermophilus maltogenic amylase (BSMA), and their molecular fine structure and susceptibility to amylolytic enzymes were investigated. By BE treatment, the molecular weight decreased from 3...
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Published in | Carbohydrate polymers Vol. 75; no. 1; pp. 9 - 14 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
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Oxford
Elsevier Ltd
01.01.2009
Elsevier Science |
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Abstract | Tapioca starch was modified using branching enzyme (BE) isolated from
Bacillus
subtilis 168 and
Bacillus stearothermophilus maltogenic amylase (BSMA), and their molecular fine structure and susceptibility to amylolytic enzymes were investigated. By BE treatment, the molecular weight decreased from 3.1
×
10
8 to 1.7
×
10
6, the number of shorter branch chains (DP 6–12) increased, the number of longer branch chains (DP >25) decreased, and amylose content decreased from 18.9% to 0.75%. This indicated that α–1,4 linkages of amylose and amylopectin were cleaved, and moiety of glycosyl residues were transferred to another amylose and amylopectin to produce branched glucan and BE-treated tapioca starch by forming α–1,6 branch linkages. The product was further modified with BSMA to produce highly-branched tapioca starch with 9.7% of extra branch points. When subject to digestion with human pancreatic α-amylase (HPA), porcine pancreatic α-amylase (PPA) and glucoamylase, highly-branched tapioca starch gave significantly lowered α-amylase susceptibility (7.5 times, 14.4 times and 3.9 times, respectively), compared to native tapioca starch. |
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AbstractList | Tapioca starch was modified using branching enzyme (BE) isolated from Bacillus subtilis 168 and Bacillus stearothermophilus maltogenic amylase (BSMA), and their molecular fine structure and susceptibility to amylolytic enzymes were investigated. By BE treatment, the molecular weight decreased from 3.1 x 10 super(8) to 1.7 x 10 super(6), the number of shorter branch chains (DP 6-12) increased, the number of longer branch chains (DP >25) decreased, and amylose content decreased from 18.9% to 0.75%. This indicated that alpha -1,4 linkages of amylose and amylopectin were cleaved, and moiety of glycosyl residues were transferred to another amylose and amylopectin to produce branched glucan and BE-treated tapioca starch by forming alpha -1,6 branch linkages. The product was further modified with BSMA to produce highly-branched tapioca starch with 9.7% of extra branch points. When subject to digestion with human pancreatic alpha -amylase (HPA), porcine pancreatic alpha - amylase (PPA) and glucoamylase, highly-branched tapioca starch gave significantly lowered alpha -amylase susceptibility (7.5 times, 14.4 times and 3.9 times, respectively), compared to native tapioca starch. Tapioca starch was modified using branching enzyme (BE) isolated from Bacillus subtilis 168 and Bacillus stearothermophilus maltogenic amylase (BSMA), and their molecular fine structure and susceptibility to amylolytic enzymes were investigated. By BE treatment, the molecular weight decreased from 3.1 × 10 8 to 1.7 × 10 6, the number of shorter branch chains (DP 6–12) increased, the number of longer branch chains (DP >25) decreased, and amylose content decreased from 18.9% to 0.75%. This indicated that α–1,4 linkages of amylose and amylopectin were cleaved, and moiety of glycosyl residues were transferred to another amylose and amylopectin to produce branched glucan and BE-treated tapioca starch by forming α–1,6 branch linkages. The product was further modified with BSMA to produce highly-branched tapioca starch with 9.7% of extra branch points. When subject to digestion with human pancreatic α-amylase (HPA), porcine pancreatic α-amylase (PPA) and glucoamylase, highly-branched tapioca starch gave significantly lowered α-amylase susceptibility (7.5 times, 14.4 times and 3.9 times, respectively), compared to native tapioca starch. Tapioca starch was modified using branching enzyme (BE) isolated from Bacillus subtilis 168 and Bacillus stearothermophilus maltogenic amylase (BSMA), and their molecular fine structure and susceptibility to amylolytic enzymes were investigated. By BE treatment, the molecular weight decreased from 3.1 x 10⁸ to 1.7 x 10⁶, the number of shorter branch chains (DP 6-12) increased, the number of longer branch chains (DP >25) decreased, and amylose content decreased from 18.9% to 0.75%. This indicated that α-1,4 linkages of amylose and amylopectin were cleaved, and moiety of glycosyl residues were transferred to another amylose and amylopectin to produce branched glucan and BE-treated tapioca starch by forming α-1,6 branch linkages. The product was further modified with BSMA to produce highly-branched tapioca starch with 9.7% of extra branch points. When subject to digestion with human pancreatic α-amylase (HPA), porcine pancreatic α-amylase (PPA) and glucoamylase, highly-branched tapioca starch gave significantly lowered α-amylase susceptibility (7.5 times, 14.4 times and 3.9 times, respectively), compared to native tapioca starch. Tapioca starch was modified using branching enzyme (BE) isolated from Bacillus subtilis 168 and Bacillus stearothermophilus maltogenic amylase (BSMA), and their molecular fine structure and susceptibility to amylolytic enzymes were investigated. By BE treatment, the molecular weight decreased from 3.1 X 108 to 1.7 X 106, the number of shorter branch chains (DP 6-12) increased, the number of longer branch chains (DP >25) decreased, and amylose content decreased from 18.9% to 0.75%. This indicated that alpha -1,4 linkages of amylose and amylopectin were cleaved, and moiety of glycosyl residues were transferred to another amylose and amylopectin to produce branched glucan and BE-treated tapioca starch by forming alpha -1,6 branch linkages. The product was further modified with BSMA to produce highly-branched tapioca starch with 9.7% of extra branch points. When subject to digestion with human pancreatic alpha -amylase (HPA), porcine pancreatic alpha -amylase (PPA) and glucoamylase, highly-branched tapioca starch gave significantly lowered alpha -amylase susceptibility (7.5 times, 14.4 times and 3.9 times, respectively), compared to native tapioca starch. |
Author | Kim, Yong-Ro Zhang, Ran Withers, Stephen G. Park, Kwan-Hwa Kim, Young-Wan Le, Quang-Tri Auh, Joong-Hyuck Lee, Chang-Kyu Lee, Seung-Jae |
Author_xml | – sequence: 1 givenname: Quang-Tri surname: Le fullname: Le, Quang-Tri organization: Center for Agricultural Biomaterials, Department of Food Science and Biotechnology, Seoul National University, Sillim-dong, Kwanak-gu, Seoul 151-742, Republic of Korea – sequence: 2 givenname: Chang-Kyu surname: Lee fullname: Lee, Chang-Kyu organization: Center for Agricultural Biomaterials, Department of Food Science and Biotechnology, Seoul National University, Sillim-dong, Kwanak-gu, Seoul 151-742, Republic of Korea – sequence: 3 givenname: Young-Wan surname: Kim fullname: Kim, Young-Wan organization: Department of Food and Biotechnology, Korea University, Jochiwon, Chungnam, 339-700, Republic of Korea – sequence: 4 givenname: Seung-Jae surname: Lee fullname: Lee, Seung-Jae organization: Center for Agricultural Biomaterials, Department of Food Science and Biotechnology, Seoul National University, Sillim-dong, Kwanak-gu, Seoul 151-742, Republic of Korea – sequence: 5 givenname: Ran surname: Zhang fullname: Zhang, Ran organization: Department of Chemistry, University of British Columbia, W300-6174 University Boulevard, Vancouver, BC V6T 1Z3, Canada – sequence: 6 givenname: Stephen G. surname: Withers fullname: Withers, Stephen G. organization: Department of Chemistry, University of British Columbia, W300-6174 University Boulevard, Vancouver, BC V6T 1Z3, Canada – sequence: 7 givenname: Yong-Ro surname: Kim fullname: Kim, Yong-Ro organization: Center for Agricultural Biomaterials, Department of Biosystems & Biomaterials Science and Engineering, Seoul National University, Sillim-dong, Kwanak-gu, Seoul 151-742, Republic of Korea – sequence: 8 givenname: Joong-Hyuck surname: Auh fullname: Auh, Joong-Hyuck email: jhauh@cau.ac.kr organization: Department of Food Science & Technology, Chung-Ang University, 72-1, Nae-ri, Daedok-Myeon, Anseong 456-756, Republic of Korea – sequence: 9 givenname: Kwan-Hwa surname: Park fullname: Park, Kwan-Hwa email: parkkh@snu.ac.kr organization: Center for Agricultural Biomaterials, Department of Food Science and Biotechnology, Seoul National University, Sillim-dong, Kwanak-gu, Seoul 151-742, Republic of Korea |
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Keywords | Highly-branched tapioca starch Branching enzyme Maltogenic amylase Biological properties Branching Amylase Molecular structure Enzyme Transferases Glycosyltransferases Resistant starch Experimental study 1,4-α-Glucan branching enzyme Transglycosylation Preparation Enzymatic digestion Oside polymer Hexosyltransferases Starch derivative Digestibility Enzymatic reaction Successive reaction |
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Snippet | Tapioca starch was modified using branching enzyme (BE) isolated from
Bacillus
subtilis 168 and
Bacillus stearothermophilus maltogenic amylase (BSMA), and... Tapioca starch was modified using branching enzyme (BE) isolated from Bacillus subtilis 168 and Bacillus stearothermophilus maltogenic amylase (BSMA), and... |
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SubjectTerms | amylases amylopectin amylose Applied sciences Bacillus stearothermophilus Bacillus subtilis Branching enzyme chemical structure enzymatic reactions enzymatic treatment enzyme activity Exact sciences and technology Highly-branched tapioca starch Maltogenic amylase modified starch molecular weight Natural polymers Physicochemistry of polymers reaction kinetics Starch and polysaccharides tapioca |
Title | Amylolytically-resistant tapioca starch modified by combined treatment of branching enzyme and maltogenic amylase |
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