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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Main Authors: Hye-Jeong Choi, Dam-Seul Ko, Na-Ri Kim, Woo-Jae Choung, Ye-Seul Koo, Da-Woon Jeong, Jae-Hoon Shim
Format: Article
Language:English
Published: Wiley 2018-01-01
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.
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language English
publishDate 2018-01-01
publisher Wiley
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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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