Evidence map›Paper›PMID 29680901›Full record

ArticleApplied microbiology and biotechnology2018

β-Mannanase-catalyzed synthesis of alkyl mannooligosides.

Johan Morrill, Anna Månberger, Anna Rosengren, Polina Naidjonoka, Pernille von Freiesleben, Kristian B R M Krogh, Karl-Erik Bergquist, Tommy Nylander, Eva Nordberg Karlsson, Patrick Adlercreutz and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
2.6field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Crystal structure of a homotrimeric verrucomicrobialJournal of structural biology: X · 2021
    Article
  3. Article
  4. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 2 countries.

Johan MorrillDepartment of Biochemistry and Structural Biology, Lund University, PO Box 124, S-221 00, Lund, Sweden.
Anna MånbergerDepartment of Biotechnology, Lund University, PO Box 124, S-221 00, Lund, Sweden.
Anna RosengrenDepartment of Biochemistry and Structural Biology, Lund University, PO Box 124, S-221 00, Lund, Sweden.
Polina NaidjonokaDepartment of Physical Chemistry, Lund University, PO Box 124, S-221 00, Lund, Sweden.
Pernille von FreieslebenNovozymes A/S, Krogshøjvej 36, 2880, Bagsværd, Denmark.
Kristian B R M KroghNovozymes A/S, Krogshøjvej 36, 2880, Bagsværd, Denmark.
Karl-Erik BergquistCentre for Analysis and Synthesis, Department of Chemistry, Lund University, PO Box 124, S-221 00, Lund, Sweden.
Tommy NylanderDepartment of Physical Chemistry, Lund University, PO Box 124, S-221 00, Lund, Sweden.
Eva Nordberg KarlssonDepartment of Biotechnology, Lund University, PO Box 124, S-221 00, Lund, Sweden.
Patrick AdlercreutzDepartment of Biotechnology, Lund University, PO Box 124, S-221 00, Lund, Sweden.
Henrik StålbrandDepartment of Biochemistry and Structural Biology, Lund University, PO Box 124, S-221 00, Lund, Sweden. henrik.stalbrand@biochemistry.lu.se.
Lund University · SENovozymes (Denmark) · DK

Funding

Stiftelsen för Strategisk Forskning RBP14-0046VINNOVA 2013-0324
6 · The paper itself

Abstract

β-Mannanases catalyze the conversion and modification of β-mannans and may, in addition to hydrolysis, also be capable of transglycosylation which can result in enzymatic synthesis of novel glycoconjugates. Using alcohols as glycosyl acceptors (alcoholysis), β-mannanases can potentially be used to synthesize alkyl glycosides, biodegradable surfactants, from renewable β-mannans. In this paper, we investigate the synthesis of alkyl mannooligosides using glycoside hydrolase family 5 β-mannanases from the fungi Trichoderma reesei (TrMan5A and TrMan5A-R171K) and Aspergillus nidulans (AnMan5C). To evaluate β-mannanase alcoholysis capacity, a novel mass spectrometry-based method was developed that allows for relative comparison of the formation of alcoholysis products using different enzymes or reaction conditions. Differences in alcoholysis capacity and potential secondary hydrolysis of alkyl mannooligosides were observed when comparing alcoholysis catalyzed by the three β-mannanases using methanol or 1-hexanol as acceptor. Among the three β-mannanases studied, TrMan5A was the most efficient in producing hexyl mannooligosides with 1-hexanol as acceptor. Hexyl mannooligosides were synthesized using TrMan5A and purified using high-performance liquid chromatography. The data suggests a high selectivity of TrMan5A for 1-hexanol as acceptor over water. The synthesized hexyl mannooligosides were structurally characterized using nuclear magnetic resonance, with results in agreement with their predicted β-conformation. The surfactant properties of the synthesized hexyl mannooligosides were evaluated using tensiometry, showing that they have similar micelle-forming properties as commercially available hexyl glucosides. The present paper demonstrates the possibility of using β-mannanases for alkyl glycoside synthesis and increases the potential utilization of renewable β-mannans.

Indexed as

Aspergillus nidulansbeta-MannosidaseGlycosidesHydrolysisMannansTrichodermabeta-MannosidaseGlycosidesMannansAlcoholysisAlkyl glycosideSurfactantTransglycosylationβ-Mannanase

Identifiers

PMID29680901
PMCPMC5959982
OpenAlexW2801952326

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.