Functional comparison of versatile carbohydrate esterases from families CE1, CE6 and CE16 on acetyl-4-O-methylglucuronoxylan and acetyl-galactoglucomannan

Galina Mai-Gisondi, Hannu Maaheimo, Sun-Li Chong, Sandra Hinz, Maija Tenkanen, Emma Master

Research output: Contribution to journalArticleScientificpeer-review

4 Citations (Scopus)

Abstract

Background The backbone structure of many hemicelluloses is acetylated, which presents a challenge when the objective is to convert corresponding polysaccharides to fermentable sugars or else recover hemicelluloses for biomaterial applications. Carbohydrate esterases (CE) can be harnessed to overcome these challenges. Methods Enzymes from different CE families, AnAcXE (CE1), OsAcXE (CE6), and MtAcE (CE16) were compared based on action and position preference towards acetyl-4-O-methylglucuronoxylan (MGX) and acetyl-galactoglucomannan (GGM). To determine corresponding positional preferences, the relative rate of acetyl group released by each enzyme was analyzed by real time 1H NMR. Results AnAcXE (CE1) showed lowest specific activity towards MGX, where OsAcXE (CE6) and MtAcE were approximately four times more active than AnAcXE (CE1). MtAcE (CE16) was further distinguished by demonstrating 100 times higher activity on GGM compared to AnAcXE (CE1) and OsAcXE (CE6), and five times higher activity on GGM than MGX. Following 24 h incubation, all enzymes removed between 78 and 93% of total acetyl content from MGX and GGM, where MtAcE performed best on both substrates. Major conclusions Considering action on MGX, all esterases showed preference for doubly substituted xylopyranosyl residues (2,3-O-acetyl-Xylp). Considering action on GGM, OsAcXE (CE6) preferentially targeted 2-O-acetyl-mannopyranosyl residues (2-O-acetyl-Manp) whereas AnAcXE (CE1) demonstrated highest activity towards 3-O-acetyl-Manp positions; regiopreference of MtAcE (CE16) on GGM was less clear. General significance The current comparative analysis identifies options to control the position of acetyl group release at initial stages of reaction, and enzyme combinations likely to accelerate deacetylation of major hemicellulose sources.
Original languageEnglish
Pages (from-to)2398-2405
Number of pages8
JournalBiochimica et Biophysica Acta: General Subjects
Volume1861
Issue number9
DOIs
Publication statusPublished - 1 Sep 2017
MoE publication typeA1 Journal article-refereed

Fingerprint

Esterases
Carbohydrates
Enzymes
Biocompatible Materials
Polysaccharides
Sugars
4-O-methyl glucuronoxylan
galactoglucomannan
O-acetylgalactoglucomannan
Nuclear magnetic resonance
Substrates
hemicellulose

Keywords

  • Acetyl (xylan) esterases
  • Acetyl-4-O-methylglucuronoxylan and acetyl-galactoglucomannan
  • carbohydrate esterase families
  • hemicellulose
  • regio-selectivity

Cite this

@article{d42e81eeb9d14de78b58dc0f49640873,
title = "Functional comparison of versatile carbohydrate esterases from families CE1, CE6 and CE16 on acetyl-4-O-methylglucuronoxylan and acetyl-galactoglucomannan",
abstract = "Background The backbone structure of many hemicelluloses is acetylated, which presents a challenge when the objective is to convert corresponding polysaccharides to fermentable sugars or else recover hemicelluloses for biomaterial applications. Carbohydrate esterases (CE) can be harnessed to overcome these challenges. Methods Enzymes from different CE families, AnAcXE (CE1), OsAcXE (CE6), and MtAcE (CE16) were compared based on action and position preference towards acetyl-4-O-methylglucuronoxylan (MGX) and acetyl-galactoglucomannan (GGM). To determine corresponding positional preferences, the relative rate of acetyl group released by each enzyme was analyzed by real time 1H NMR. Results AnAcXE (CE1) showed lowest specific activity towards MGX, where OsAcXE (CE6) and MtAcE were approximately four times more active than AnAcXE (CE1). MtAcE (CE16) was further distinguished by demonstrating 100 times higher activity on GGM compared to AnAcXE (CE1) and OsAcXE (CE6), and five times higher activity on GGM than MGX. Following 24 h incubation, all enzymes removed between 78 and 93{\%} of total acetyl content from MGX and GGM, where MtAcE performed best on both substrates. Major conclusions Considering action on MGX, all esterases showed preference for doubly substituted xylopyranosyl residues (2,3-O-acetyl-Xylp). Considering action on GGM, OsAcXE (CE6) preferentially targeted 2-O-acetyl-mannopyranosyl residues (2-O-acetyl-Manp) whereas AnAcXE (CE1) demonstrated highest activity towards 3-O-acetyl-Manp positions; regiopreference of MtAcE (CE16) on GGM was less clear. General significance The current comparative analysis identifies options to control the position of acetyl group release at initial stages of reaction, and enzyme combinations likely to accelerate deacetylation of major hemicellulose sources.",
keywords = "Acetyl (xylan) esterases, Acetyl-4-O-methylglucuronoxylan and acetyl-galactoglucomannan, carbohydrate esterase families, hemicellulose, regio-selectivity",
author = "Galina Mai-Gisondi and Hannu Maaheimo and Sun-Li Chong and Sandra Hinz and Maija Tenkanen and Emma Master",
year = "2017",
month = "9",
day = "1",
doi = "10.1016/j.bbagen.2017.06.002",
language = "English",
volume = "1861",
pages = "2398--2405",
journal = "Biochimica et Biophysica Acta: General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "9",

}

Functional comparison of versatile carbohydrate esterases from families CE1, CE6 and CE16 on acetyl-4-O-methylglucuronoxylan and acetyl-galactoglucomannan. / Mai-Gisondi, Galina; Maaheimo, Hannu; Chong, Sun-Li; Hinz, Sandra; Tenkanen, Maija; Master, Emma.

In: Biochimica et Biophysica Acta: General Subjects, Vol. 1861, No. 9, 01.09.2017, p. 2398-2405.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Functional comparison of versatile carbohydrate esterases from families CE1, CE6 and CE16 on acetyl-4-O-methylglucuronoxylan and acetyl-galactoglucomannan

AU - Mai-Gisondi, Galina

AU - Maaheimo, Hannu

AU - Chong, Sun-Li

AU - Hinz, Sandra

AU - Tenkanen, Maija

AU - Master, Emma

PY - 2017/9/1

Y1 - 2017/9/1

N2 - Background The backbone structure of many hemicelluloses is acetylated, which presents a challenge when the objective is to convert corresponding polysaccharides to fermentable sugars or else recover hemicelluloses for biomaterial applications. Carbohydrate esterases (CE) can be harnessed to overcome these challenges. Methods Enzymes from different CE families, AnAcXE (CE1), OsAcXE (CE6), and MtAcE (CE16) were compared based on action and position preference towards acetyl-4-O-methylglucuronoxylan (MGX) and acetyl-galactoglucomannan (GGM). To determine corresponding positional preferences, the relative rate of acetyl group released by each enzyme was analyzed by real time 1H NMR. Results AnAcXE (CE1) showed lowest specific activity towards MGX, where OsAcXE (CE6) and MtAcE were approximately four times more active than AnAcXE (CE1). MtAcE (CE16) was further distinguished by demonstrating 100 times higher activity on GGM compared to AnAcXE (CE1) and OsAcXE (CE6), and five times higher activity on GGM than MGX. Following 24 h incubation, all enzymes removed between 78 and 93% of total acetyl content from MGX and GGM, where MtAcE performed best on both substrates. Major conclusions Considering action on MGX, all esterases showed preference for doubly substituted xylopyranosyl residues (2,3-O-acetyl-Xylp). Considering action on GGM, OsAcXE (CE6) preferentially targeted 2-O-acetyl-mannopyranosyl residues (2-O-acetyl-Manp) whereas AnAcXE (CE1) demonstrated highest activity towards 3-O-acetyl-Manp positions; regiopreference of MtAcE (CE16) on GGM was less clear. General significance The current comparative analysis identifies options to control the position of acetyl group release at initial stages of reaction, and enzyme combinations likely to accelerate deacetylation of major hemicellulose sources.

AB - Background The backbone structure of many hemicelluloses is acetylated, which presents a challenge when the objective is to convert corresponding polysaccharides to fermentable sugars or else recover hemicelluloses for biomaterial applications. Carbohydrate esterases (CE) can be harnessed to overcome these challenges. Methods Enzymes from different CE families, AnAcXE (CE1), OsAcXE (CE6), and MtAcE (CE16) were compared based on action and position preference towards acetyl-4-O-methylglucuronoxylan (MGX) and acetyl-galactoglucomannan (GGM). To determine corresponding positional preferences, the relative rate of acetyl group released by each enzyme was analyzed by real time 1H NMR. Results AnAcXE (CE1) showed lowest specific activity towards MGX, where OsAcXE (CE6) and MtAcE were approximately four times more active than AnAcXE (CE1). MtAcE (CE16) was further distinguished by demonstrating 100 times higher activity on GGM compared to AnAcXE (CE1) and OsAcXE (CE6), and five times higher activity on GGM than MGX. Following 24 h incubation, all enzymes removed between 78 and 93% of total acetyl content from MGX and GGM, where MtAcE performed best on both substrates. Major conclusions Considering action on MGX, all esterases showed preference for doubly substituted xylopyranosyl residues (2,3-O-acetyl-Xylp). Considering action on GGM, OsAcXE (CE6) preferentially targeted 2-O-acetyl-mannopyranosyl residues (2-O-acetyl-Manp) whereas AnAcXE (CE1) demonstrated highest activity towards 3-O-acetyl-Manp positions; regiopreference of MtAcE (CE16) on GGM was less clear. General significance The current comparative analysis identifies options to control the position of acetyl group release at initial stages of reaction, and enzyme combinations likely to accelerate deacetylation of major hemicellulose sources.

KW - Acetyl (xylan) esterases

KW - Acetyl-4-O-methylglucuronoxylan and acetyl-galactoglucomannan

KW - carbohydrate esterase families

KW - hemicellulose

KW - regio-selectivity

UR - http://www.scopus.com/inward/record.url?scp=85022188809&partnerID=8YFLogxK

U2 - 10.1016/j.bbagen.2017.06.002

DO - 10.1016/j.bbagen.2017.06.002

M3 - Article

VL - 1861

SP - 2398

EP - 2405

JO - Biochimica et Biophysica Acta: General Subjects

JF - Biochimica et Biophysica Acta: General Subjects

SN - 0304-4165

IS - 9

ER -