Preparative and Kinetic Analysis of β-1,4- and β-1,3-Glucan Phosphorylases Informs Access to Human Milk Oligosaccharide Fragments and Analogues ThereofCitation formats

  • External authors:
  • Ravindra Pal Singh
  • Giulia Pergolizzi
  • Sergey A Nepogodiev
  • Peterson de Andrade
  • Sakonwan Kuhaudomlarp

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Preparative and Kinetic Analysis of β-1,4- and β-1,3-Glucan Phosphorylases Informs Access to Human Milk Oligosaccharide Fragments and Analogues Thereof. / Singh, Ravindra Pal; Pergolizzi, Giulia; Nepogodiev, Sergey A; de Andrade, Peterson; Kuhaudomlarp, Sakonwan; Field, Robert A.

In: CHEMBIOCHEM, Vol. 21, No. 7, 01.04.2020, p. 1043-1049.

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Author

Singh, Ravindra Pal ; Pergolizzi, Giulia ; Nepogodiev, Sergey A ; de Andrade, Peterson ; Kuhaudomlarp, Sakonwan ; Field, Robert A. / Preparative and Kinetic Analysis of β-1,4- and β-1,3-Glucan Phosphorylases Informs Access to Human Milk Oligosaccharide Fragments and Analogues Thereof. In: CHEMBIOCHEM. 2020 ; Vol. 21, No. 7. pp. 1043-1049.

Bibtex

@article{7948a036c01940f1be89f6dc28d6cc9b,
title = "Preparative and Kinetic Analysis of β-1,4- and β-1,3-Glucan Phosphorylases Informs Access to Human Milk Oligosaccharide Fragments and Analogues Thereof",
abstract = "The enzymatic synthesis of oligosaccharides depends on the availability of suitable enzymes, which remains a limitation. Without recourse to enzyme engineering or evolution approaches, herein we demonstrate the ability of wild-type cellodextrin phosphorylase (CDP: β-1,4-glucan linkage-dependent) and laminaridextrin phosphorylase (Pro_7066: β-1,3-glucan linkage-dependent) to tolerate a number of sugar-1- phosphate substrates, albeit with reduced kinetic efficiency. In spite of catalytic efficiencies of <1 % of the natural reactions, we demonstrate the utility of given phosphorylase-sugar phosphate pairs to access new-to-nature fragments of human milk oligosaccharides, or analogues thereof, in multi-milligram quantities.",
author = "Singh, {Ravindra Pal} and Giulia Pergolizzi and Nepogodiev, {Sergey A} and {de Andrade}, Peterson and Sakonwan Kuhaudomlarp and Field, {Robert A}",
note = "{\textcopyright} 2019 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.",
year = "2020",
month = apr,
day = "1",
doi = "10.1002/cbic.201900440",
language = "English",
volume = "21",
pages = "1043--1049",
journal = "ChemBioChem: a European journal of chemical biology ",
issn = "1439-4227",
publisher = "John Wiley & Sons Ltd",
number = "7",

}

RIS

TY - JOUR

T1 - Preparative and Kinetic Analysis of β-1,4- and β-1,3-Glucan Phosphorylases Informs Access to Human Milk Oligosaccharide Fragments and Analogues Thereof

AU - Singh, Ravindra Pal

AU - Pergolizzi, Giulia

AU - Nepogodiev, Sergey A

AU - de Andrade, Peterson

AU - Kuhaudomlarp, Sakonwan

AU - Field, Robert A

N1 - © 2019 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.

PY - 2020/4/1

Y1 - 2020/4/1

N2 - The enzymatic synthesis of oligosaccharides depends on the availability of suitable enzymes, which remains a limitation. Without recourse to enzyme engineering or evolution approaches, herein we demonstrate the ability of wild-type cellodextrin phosphorylase (CDP: β-1,4-glucan linkage-dependent) and laminaridextrin phosphorylase (Pro_7066: β-1,3-glucan linkage-dependent) to tolerate a number of sugar-1- phosphate substrates, albeit with reduced kinetic efficiency. In spite of catalytic efficiencies of <1 % of the natural reactions, we demonstrate the utility of given phosphorylase-sugar phosphate pairs to access new-to-nature fragments of human milk oligosaccharides, or analogues thereof, in multi-milligram quantities.

AB - The enzymatic synthesis of oligosaccharides depends on the availability of suitable enzymes, which remains a limitation. Without recourse to enzyme engineering or evolution approaches, herein we demonstrate the ability of wild-type cellodextrin phosphorylase (CDP: β-1,4-glucan linkage-dependent) and laminaridextrin phosphorylase (Pro_7066: β-1,3-glucan linkage-dependent) to tolerate a number of sugar-1- phosphate substrates, albeit with reduced kinetic efficiency. In spite of catalytic efficiencies of <1 % of the natural reactions, we demonstrate the utility of given phosphorylase-sugar phosphate pairs to access new-to-nature fragments of human milk oligosaccharides, or analogues thereof, in multi-milligram quantities.

U2 - 10.1002/cbic.201900440

DO - 10.1002/cbic.201900440

M3 - Article

C2 - 31657512

VL - 21

SP - 1043

EP - 1049

JO - ChemBioChem: a European journal of chemical biology

JF - ChemBioChem: a European journal of chemical biology

SN - 1439-4227

IS - 7

ER -