Colorimetric detection of acetyl xylan esterase activities

Galina Mai-Gisondi; Emma R. Master

doi:10.1007/978-1-4939-6899-2_5

Colorimetric detection of acetyl xylan esterase activities

Galina Mai-Gisondi, Emma R. Master^*

^*Corresponding author for this work

University of Toronto

Research output: Chapter in Book/Report/Conference proceeding › Chapter › Scientific › peer-review

9 Citations (Scopus)

Abstract

Colorimetric detection of reaction products is typically preferred for initial surveys of acetyl xylan esterase (AcXE) activity. This chapter will describe common colorimetric methods, and variations thereof, for measuring AcXE activities on commercial, synthesized, and natural substrates. Whereas assays using pNP-acetate, α-naphthyl acetate, and 4-methylumbelliferyl acetate (4MUA) are emphasized, common methods used to measure AcXE activity towards carbohydrate analogs (e.g., acetylated p-nitrophenyl β-d-xylopyranosides) and various acetylated xylans are also described. Strengths and limitations of the colorimetric assays are highlighted.

Original language	English
Title of host publication	Protein-Carbohydrate Interactions
Subtitle of host publication	Methods and Protocols
Editors	D. Wade Abbott, Alicia Lammerts van Bueren
Publisher	Springer
Pages	45-57
Number of pages	13
ISBN (Electronic)	978-1-4939-6899-2
ISBN (Print)	978-1-4939-6898-5
DOIs	https://doi.org/10.1007/978-1-4939-6899-2_5
Publication status	Published - 2017
MoE publication type	A3 Book section, Chapters in research books

Publication series

Name	Methods in Molecular Biology
Volume	1588
ISSN (Print)	10643745

Keywords

4-Methylumbelliferyl acetate
Acetyl xylan esterase
Acetylated xylooligosaccharides
Colorimetric assays
pNP-acetate
α-Naphthyl acetate
β-Xylosidase-coupled assay

Access to Document

10.1007/978-1-4939-6899-2_5

Cite this

@inbook{cbb986cfe365475f9237a99e548d74c8,

title = "Colorimetric detection of acetyl xylan esterase activities",

abstract = "Colorimetric detection of reaction products is typically preferred for initial surveys of acetyl xylan esterase (AcXE) activity. This chapter will describe common colorimetric methods, and variations thereof, for measuring AcXE activities on commercial, synthesized, and natural substrates. Whereas assays using pNP-acetate, α-naphthyl acetate, and 4-methylumbelliferyl acetate (4MUA) are emphasized, common methods used to measure AcXE activity towards carbohydrate analogs (e.g., acetylated p-nitrophenyl β-d-xylopyranosides) and various acetylated xylans are also described. Strengths and limitations of the colorimetric assays are highlighted.",

keywords = "4-Methylumbelliferyl acetate, Acetyl xylan esterase, Acetylated xylooligosaccharides, Colorimetric assays, pNP-acetate, α-Naphthyl acetate, β-Xylosidase-coupled assay",

author = "Galina Mai-Gisondi and Master, {Emma R.}",

note = "| openaire: EC/H2020/33947/EU//BHIVE",

year = "2017",

doi = "10.1007/978-1-4939-6899-2_5",

language = "English",

isbn = "978-1-4939-6898-5",

series = "Methods in Molecular Biology",

publisher = "Springer",

pages = "45--57",

editor = "Abbott, {D. Wade} and {Lammerts van Bueren}, Alicia",

booktitle = "Protein-Carbohydrate Interactions",

address = "Germany",

}

Colorimetric detection of acetyl xylan esterase activities. / Mai-Gisondi, Galina; Master, Emma R.
Protein-Carbohydrate Interactions: Methods and Protocols. ed. / D. Wade Abbott; Alicia Lammerts van Bueren. Springer, 2017. p. 45-57 (Methods in Molecular Biology; Vol. 1588).

Research output: Chapter in Book/Report/Conference proceeding › Chapter › Scientific › peer-review

TY - CHAP

T1 - Colorimetric detection of acetyl xylan esterase activities

AU - Mai-Gisondi, Galina

AU - Master, Emma R.

N1 - | openaire: EC/H2020/33947/EU//BHIVE

PY - 2017

Y1 - 2017

N2 - Colorimetric detection of reaction products is typically preferred for initial surveys of acetyl xylan esterase (AcXE) activity. This chapter will describe common colorimetric methods, and variations thereof, for measuring AcXE activities on commercial, synthesized, and natural substrates. Whereas assays using pNP-acetate, α-naphthyl acetate, and 4-methylumbelliferyl acetate (4MUA) are emphasized, common methods used to measure AcXE activity towards carbohydrate analogs (e.g., acetylated p-nitrophenyl β-d-xylopyranosides) and various acetylated xylans are also described. Strengths and limitations of the colorimetric assays are highlighted.

AB - Colorimetric detection of reaction products is typically preferred for initial surveys of acetyl xylan esterase (AcXE) activity. This chapter will describe common colorimetric methods, and variations thereof, for measuring AcXE activities on commercial, synthesized, and natural substrates. Whereas assays using pNP-acetate, α-naphthyl acetate, and 4-methylumbelliferyl acetate (4MUA) are emphasized, common methods used to measure AcXE activity towards carbohydrate analogs (e.g., acetylated p-nitrophenyl β-d-xylopyranosides) and various acetylated xylans are also described. Strengths and limitations of the colorimetric assays are highlighted.

KW - 4-Methylumbelliferyl acetate

KW - Acetyl xylan esterase

KW - Acetylated xylooligosaccharides

KW - Colorimetric assays

KW - pNP-acetate

KW - α-Naphthyl acetate

KW - β-Xylosidase-coupled assay

UR - http://www.scopus.com/inward/record.url?scp=85018549020&partnerID=8YFLogxK

U2 - 10.1007/978-1-4939-6899-2_5

DO - 10.1007/978-1-4939-6899-2_5

M3 - Chapter

C2 - 28417360

AN - SCOPUS:85018549020

SN - 978-1-4939-6898-5

T3 - Methods in Molecular Biology

SP - 45

EP - 57

BT - Protein-Carbohydrate Interactions

A2 - Abbott, D. Wade

A2 - Lammerts van Bueren, Alicia

PB - Springer

ER -

Colorimetric detection of acetyl xylan esterase activities

Abstract

Publication series

Keywords

Access to Document

Other files and links

Fingerprint

BHIVE: Bio-derived HIgh Value polymers through novel Enzyme function

Cite this

Colorimetric detection of acetyl xylan esterase activities

Abstract

Publication series

Keywords

Access to Document

Other files and links

Fingerprint

Projects

BHIVE: Bio-derived HIgh Value polymers through novel Enzyme function

Cite this