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

Research output: Contribution to journalArticleScientificpeer-review

Researchers

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

Research units

  • University of Toronto
  • VTT Technical Research Centre of Finland
  • University of Helsinki
  • DuPont Industrial Biosciences

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-Xyl. p). Considering action on GGM, OsAcXE (CE6) preferentially targeted 2-O-acetyl-mannopyranosyl residues (2-O-acetyl-Man. p) whereas AnAcXE (CE1) demonstrated highest activity towards 3-O-acetyl-Man. p 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.

Details

Original languageEnglish
Pages (from-to)2398-2405
JournalBIOCHIMICA ET BIOPHYSICA ACTA: GENERAL SUBJECTS
Volume1861
Issue number9
Early online date2017
Publication statusPublished - Sep 2017
MoE publication typeA1 Journal article-refereed

    Research areas

  • Acetyl (xylan) esterases, Acetyl-4-O-methylglucuronoxylan and acetyl-galactoglucomannan, Carbohydrate esterase families, Hemicellulose, Regio-selectivity

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