Complex formation of a 4-a-glucanotransferase using starch as a biocatalyst for starch modification
A 4-a-glucanotransferases from Thermus thermophilus (TTaGT) possesses an extra substrate binding site, leading to facile purification of the intact enzyme using amylose as an insoluble binding matrix. Due to the cost of amylose and low recovery yield, starch was replaced for amylose as an alternativ...
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| Published in | Food science and biotechnology pp. 1659 - 1666 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
한국식품과학회
01.12.2017
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| Subjects | |
| Online Access | Get full text |
| ISSN | 1226-7708 2092-6456 |
| DOI | 10.1007/s10068-017-0203-2 |
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| Abstract | A 4-a-glucanotransferases from Thermus thermophilus (TTaGT) possesses an extra substrate binding site, leading to facile purification of the intact enzyme using amylose as an insoluble binding matrix. Due to the cost of amylose and low recovery yield, starch was replaced for amylose as an alternative capturer in this study. Using gelatinized corn starch at pH 9 with 36-h incubation in the presence of 1 M ammonium sulfate increased the TTaGT-starch complex formation yield from 2 to 56%. In preparative-scale production, TTaGT produced in Bacillus subtilis was recovered by 42.1% with the same specific activity as that of purified TTaGT. Structural and rheological analyses of the enzymatically modified starches revealed that the starch complex exhibited catalytic performance comparable to soluble TTaGT, suggesting that the starch complex can be used as a biocatalyst for modified starch production without elution of the enzyme from the complex. KCI Citation Count: 3 |
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| AbstractList | A 4-a-glucanotransferases from Thermus thermophilus (TTaGT) possesses an extra substrate binding site, leading to facile purification of the intact enzyme using amylose as an insoluble binding matrix. Due to the cost of amylose and low recovery yield, starch was replaced for amylose as an alternative capturer in this study. Using gelatinized corn starch at pH 9 with 36-h incubation in the presence of 1 M ammonium sulfate increased the TTaGT-starch complex formation yield from 2 to 56%. In preparative-scale production, TTaGT produced in Bacillus subtilis was recovered by 42.1% with the same specific activity as that of purified TTaGT. Structural and rheological analyses of the enzymatically modified starches revealed that the starch complex exhibited catalytic performance comparable to soluble TTaGT, suggesting that the starch complex can be used as a biocatalyst for modified starch production without elution of the enzyme from the complex. KCI Citation Count: 3 |
| Author | 오유경 윤선희 박지용 김영완 김용노 한상익 |
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| Title | Complex formation of a 4-a-glucanotransferase using starch as a biocatalyst for starch modification |
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