Enzymatic synthesis of a galactose-containing trehalose analogue disaccharide by Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase: Inhibitory effects on several disaccharidase activities

Hye Min Kim; You Kyung Chang; Soo In Ryu; Sung Gweon Moon; Soo Bok Lee

doi:10.1016/j.molcatb.2007.08.012

Enzymatic synthesis of a galactose-containing trehalose analogue disaccharide by Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase: Inhibitory effects on several disaccharidase activities

Hye Min Kim, You Kyung Chang, Soo In Ryu, Sung Gweon Moon, Soo Bok Lee

Department of Food and Nutrition

Research output: Contribution to journal › Article › peer-review

21 Citations (Scopus)

Abstract

Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase employed a galactose as an acceptor in the glucosyl transfer reaction with an NDP-Glc donor. The reaction produced a non-reducing transfer product in a yield of more than 30% based on the molar concentration of donor used. The transfer product was purified by paper chromatography and preparative HPLC, and its glycosidic structure was confirmed by ¹³C nuclear magnetic resonance to be α-d-glucopyranosyl α-d-galactopyranoside. Interestingly, this trehalose analogue disaccharide inhibited the action of several disaccharidases, including a trehalase. The analogue competitively inhibited porcine kidney and rat intestinal trehalases with K_i values of 0.68 and 3.7 mM, respectively. It also competitively inhibited other intestinal disaccharidases such as sucrase, maltase, and isomaltase with respective K_i values of approximately 0.66, 3.0, and 2.1 mM. Accordingly, this trehalose analogue would be a potentially indigestible disaccharide, effectively inhibiting intestinal brush border disaccharidases.

Original language	English
Pages (from-to)	98-103
Number of pages	6
Journal	Journal of Molecular Catalysis B: Enzymatic
Volume	49
Issue number	1-4
DOIs	https://doi.org/10.1016/j.molcatb.2007.08.012
Publication status	Published - 2007 Nov 16

Bibliographical note

Funding Information:
This work was supported by a grant from the Korea Research Foundation (KRF-2006-F00075), and in part by the Marine and Extreme Genome Research Center Program, Ministry of Maritime Affairs and Fisheries, Republic of Korea. We thank the Brain Korea 21 Project, Yonsei University, for financial support in the form of scholarships to H.-M. Kim and S.-I. Ryu.

All Science Journal Classification (ASJC) codes

Catalysis
Bioengineering
Biochemistry
Process Chemistry and Technology

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Kim, H. M., Chang, Y. K., Ryu, S. I., Moon, S. G., & Lee, S. B. (2007). Enzymatic synthesis of a galactose-containing trehalose analogue disaccharide by Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase: Inhibitory effects on several disaccharidase activities. Journal of Molecular Catalysis B: Enzymatic, 49(1-4), 98-103. https://doi.org/10.1016/j.molcatb.2007.08.012

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title = "Enzymatic synthesis of a galactose-containing trehalose analogue disaccharide by Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase: Inhibitory effects on several disaccharidase activities",

abstract = "Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase employed a galactose as an acceptor in the glucosyl transfer reaction with an NDP-Glc donor. The reaction produced a non-reducing transfer product in a yield of more than 30% based on the molar concentration of donor used. The transfer product was purified by paper chromatography and preparative HPLC, and its glycosidic structure was confirmed by 13C nuclear magnetic resonance to be α-d-glucopyranosyl α-d-galactopyranoside. Interestingly, this trehalose analogue disaccharide inhibited the action of several disaccharidases, including a trehalase. The analogue competitively inhibited porcine kidney and rat intestinal trehalases with Ki values of 0.68 and 3.7 mM, respectively. It also competitively inhibited other intestinal disaccharidases such as sucrase, maltase, and isomaltase with respective Ki values of approximately 0.66, 3.0, and 2.1 mM. Accordingly, this trehalose analogue would be a potentially indigestible disaccharide, effectively inhibiting intestinal brush border disaccharidases.",

author = "Kim, {Hye Min} and Chang, {You Kyung} and Ryu, {Soo In} and Moon, {Sung Gweon} and Lee, {Soo Bok}",

note = "Funding Information: This work was supported by a grant from the Korea Research Foundation (KRF-2006-F00075), and in part by the Marine and Extreme Genome Research Center Program, Ministry of Maritime Affairs and Fisheries, Republic of Korea. We thank the Brain Korea 21 Project, Yonsei University, for financial support in the form of scholarships to H.-M. Kim and S.-I. Ryu. ",

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Kim, HM, Chang, YK, Ryu, SI, Moon, SG & Lee, SB 2007, 'Enzymatic synthesis of a galactose-containing trehalose analogue disaccharide by Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase: Inhibitory effects on several disaccharidase activities', Journal of Molecular Catalysis B: Enzymatic, vol. 49, no. 1-4, pp. 98-103. https://doi.org/10.1016/j.molcatb.2007.08.012

Enzymatic synthesis of a galactose-containing trehalose analogue disaccharide by Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase: Inhibitory effects on several disaccharidase activities. / Kim, Hye Min; Chang, You Kyung; Ryu, Soo In et al.
In: Journal of Molecular Catalysis B: Enzymatic, Vol. 49, No. 1-4, 16.11.2007, p. 98-103.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Enzymatic synthesis of a galactose-containing trehalose analogue disaccharide by Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase

T2 - Inhibitory effects on several disaccharidase activities

AU - Kim, Hye Min

AU - Chang, You Kyung

AU - Ryu, Soo In

AU - Moon, Sung Gweon

AU - Lee, Soo Bok

N1 - Funding Information: This work was supported by a grant from the Korea Research Foundation (KRF-2006-F00075), and in part by the Marine and Extreme Genome Research Center Program, Ministry of Maritime Affairs and Fisheries, Republic of Korea. We thank the Brain Korea 21 Project, Yonsei University, for financial support in the form of scholarships to H.-M. Kim and S.-I. Ryu.

PY - 2007/11/16

Y1 - 2007/11/16

N2 - Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase employed a galactose as an acceptor in the glucosyl transfer reaction with an NDP-Glc donor. The reaction produced a non-reducing transfer product in a yield of more than 30% based on the molar concentration of donor used. The transfer product was purified by paper chromatography and preparative HPLC, and its glycosidic structure was confirmed by 13C nuclear magnetic resonance to be α-d-glucopyranosyl α-d-galactopyranoside. Interestingly, this trehalose analogue disaccharide inhibited the action of several disaccharidases, including a trehalase. The analogue competitively inhibited porcine kidney and rat intestinal trehalases with Ki values of 0.68 and 3.7 mM, respectively. It also competitively inhibited other intestinal disaccharidases such as sucrase, maltase, and isomaltase with respective Ki values of approximately 0.66, 3.0, and 2.1 mM. Accordingly, this trehalose analogue would be a potentially indigestible disaccharide, effectively inhibiting intestinal brush border disaccharidases.

AB - Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase employed a galactose as an acceptor in the glucosyl transfer reaction with an NDP-Glc donor. The reaction produced a non-reducing transfer product in a yield of more than 30% based on the molar concentration of donor used. The transfer product was purified by paper chromatography and preparative HPLC, and its glycosidic structure was confirmed by 13C nuclear magnetic resonance to be α-d-glucopyranosyl α-d-galactopyranoside. Interestingly, this trehalose analogue disaccharide inhibited the action of several disaccharidases, including a trehalase. The analogue competitively inhibited porcine kidney and rat intestinal trehalases with Ki values of 0.68 and 3.7 mM, respectively. It also competitively inhibited other intestinal disaccharidases such as sucrase, maltase, and isomaltase with respective Ki values of approximately 0.66, 3.0, and 2.1 mM. Accordingly, this trehalose analogue would be a potentially indigestible disaccharide, effectively inhibiting intestinal brush border disaccharidases.

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Enzymatic synthesis of a galactose-containing trehalose analogue disaccharide by Pyrococcus horikoshii trehalose-synthesizing glycosyltransferase: Inhibitory effects on several disaccharidase activities

Abstract

Bibliographical note

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