Transglycosylation Properties of a Novel α-1,4-Glucanotransferase from Bacteroides thetaiotaomicron and Its Application in Developing an α-Glucosidase-Specific Inhibitor
In this study, α-glucanotransferase from Bacteroides thetaiotaomicron was expressed in Escherichia coli and characterized. Conserved amino-acid sequence alignment showed that Bacteroides thetaiotaomicron α-glucanotransferase (BtαGTase) belongs to the glycoside hydrolase family 77. The enzyme exhibit...
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| Format: | Article |
| Language: | English |
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Wiley
2018-01-01
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| Series: | Journal of Chemistry |
| Online Access: | http://dx.doi.org/10.1155/2018/2981596 |
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| author | Hye-Jeong Choi Dam-Seul Ko Na-Ri Kim Woo-Jae Choung Ye-Seul Koo Da-Woon Jeong Jae-Hoon Shim |
| author_facet | Hye-Jeong Choi Dam-Seul Ko Na-Ri Kim Woo-Jae Choung Ye-Seul Koo Da-Woon Jeong Jae-Hoon Shim |
| author_sort | Hye-Jeong Choi |
| collection | DOAJ |
| description | In this study, α-glucanotransferase from Bacteroides thetaiotaomicron was expressed in Escherichia coli and characterized. Conserved amino-acid sequence alignment showed that Bacteroides thetaiotaomicron α-glucanotransferase (BtαGTase) belongs to the glycoside hydrolase family 77. The enzyme exhibited optimal catalytic activity at 60°C and pH 3.0. BtαGTase catalyzed transglycosylation reactions that produced only glycosyl or maltosyl transfer products, which are preferable for the generation of transglycosylated products with high yield. The 1-deoxynojirimycin (DNJ) glycosylation product G1-DNJ was generated using BtαGTase, and the inhibitory effect of G1-DNJ was analyzed. A kinetic study of inhibition revealed that G1-DNJ inhibited α-glucosidase to a greater extent than did DNJ but did not show any inhibitory effects towards α-amylase, suggesting that G1-DNJ is a potential candidate for the prevention of diabetes. |
| format | Article |
| id | doaj-art-ec4cbaa222ef4d4d9c369d94e95d5b4b |
| institution | OA Journals |
| issn | 2090-9063 2090-9071 |
| language | English |
| publishDate | 2018-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Journal of Chemistry |
| spelling | doaj-art-ec4cbaa222ef4d4d9c369d94e95d5b4b2025-08-20T02:21:47ZengWileyJournal of Chemistry2090-90632090-90712018-01-01201810.1155/2018/29815962981596Transglycosylation Properties of a Novel α-1,4-Glucanotransferase from Bacteroides thetaiotaomicron and Its Application in Developing an α-Glucosidase-Specific InhibitorHye-Jeong Choi0Dam-Seul Ko1Na-Ri Kim2Woo-Jae Choung3Ye-Seul Koo4Da-Woon Jeong5Jae-Hoon Shim6Department of Food Science and Nutrition and Center for Aging and Health Care, Hallym University, Hallymdaehak-gil 1, Chuncheon, Gangwon-do 24252, Republic of KoreaDepartment of Food Science and Nutrition and Center for Aging and Health Care, Hallym University, Hallymdaehak-gil 1, Chuncheon, Gangwon-do 24252, Republic of KoreaDepartment of Food Science and Nutrition and Center for Aging and Health Care, Hallym University, Hallymdaehak-gil 1, Chuncheon, Gangwon-do 24252, Republic of KoreaDepartment of Food Science and Nutrition and Center for Aging and Health Care, Hallym University, Hallymdaehak-gil 1, Chuncheon, Gangwon-do 24252, Republic of KoreaDepartment of Food Science and Nutrition and Center for Aging and Health Care, Hallym University, Hallymdaehak-gil 1, Chuncheon, Gangwon-do 24252, Republic of KoreaDepartment of Food Science and Nutrition and Center for Aging and Health Care, Hallym University, Hallymdaehak-gil 1, Chuncheon, Gangwon-do 24252, Republic of KoreaDepartment of Food Science and Nutrition and Center for Aging and Health Care, Hallym University, Hallymdaehak-gil 1, Chuncheon, Gangwon-do 24252, Republic of KoreaIn this study, α-glucanotransferase from Bacteroides thetaiotaomicron was expressed in Escherichia coli and characterized. Conserved amino-acid sequence alignment showed that Bacteroides thetaiotaomicron α-glucanotransferase (BtαGTase) belongs to the glycoside hydrolase family 77. The enzyme exhibited optimal catalytic activity at 60°C and pH 3.0. BtαGTase catalyzed transglycosylation reactions that produced only glycosyl or maltosyl transfer products, which are preferable for the generation of transglycosylated products with high yield. The 1-deoxynojirimycin (DNJ) glycosylation product G1-DNJ was generated using BtαGTase, and the inhibitory effect of G1-DNJ was analyzed. A kinetic study of inhibition revealed that G1-DNJ inhibited α-glucosidase to a greater extent than did DNJ but did not show any inhibitory effects towards α-amylase, suggesting that G1-DNJ is a potential candidate for the prevention of diabetes.http://dx.doi.org/10.1155/2018/2981596 |
| spellingShingle | Hye-Jeong Choi Dam-Seul Ko Na-Ri Kim Woo-Jae Choung Ye-Seul Koo Da-Woon Jeong Jae-Hoon Shim Transglycosylation Properties of a Novel α-1,4-Glucanotransferase from Bacteroides thetaiotaomicron and Its Application in Developing an α-Glucosidase-Specific Inhibitor Journal of Chemistry |
| title | Transglycosylation Properties of a Novel α-1,4-Glucanotransferase from Bacteroides thetaiotaomicron and Its Application in Developing an α-Glucosidase-Specific Inhibitor |
| title_full | Transglycosylation Properties of a Novel α-1,4-Glucanotransferase from Bacteroides thetaiotaomicron and Its Application in Developing an α-Glucosidase-Specific Inhibitor |
| title_fullStr | Transglycosylation Properties of a Novel α-1,4-Glucanotransferase from Bacteroides thetaiotaomicron and Its Application in Developing an α-Glucosidase-Specific Inhibitor |
| title_full_unstemmed | Transglycosylation Properties of a Novel α-1,4-Glucanotransferase from Bacteroides thetaiotaomicron and Its Application in Developing an α-Glucosidase-Specific Inhibitor |
| title_short | Transglycosylation Properties of a Novel α-1,4-Glucanotransferase from Bacteroides thetaiotaomicron and Its Application in Developing an α-Glucosidase-Specific Inhibitor |
| title_sort | transglycosylation properties of a novel α 1 4 glucanotransferase from bacteroides thetaiotaomicron and its application in developing an α glucosidase specific inhibitor |
| url | http://dx.doi.org/10.1155/2018/2981596 |
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