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

    10 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
    JournalBiochimica et Biophysica Acta: General Subjects
    Volume1861
    Issue number9
    DOIs
    Publication statusPublished - 1 Sep 2017
    MoE publication typeA1 Journal article-refereed

    Keywords

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

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