ArticleBeilstein journal of organic chemistry2017
Selective enzymatic esterification of lignin model compounds in the ball mill.
Article in Beilstein journal of organic chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Strategies Toward Synthesis and Conversion of Lignin Model Compounds.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Review
- Mechanochemistry for Organic and Inorganic Synthesis.ACS organic & inorganic Au · 2024Review
- Mechanocatalytic Hydrogenolysis of the Lignin Model Dimer Benzyl Phenyl Ether over Supported Palladium Catalysts.ACS sustainable chemistry & engineering · 2024Article
- The Biomodified Lignin Platform: A Review.Polymers · 2023Review
- Selective Enzymatic Esterification of Lignin-Derived Phenolics for the Synthesis of Lipophilic Antioxidants.Antioxidants (Basel, Switzerland) · 2023Article
- Biocatalytic selective acylation of technical lignins: a new route for the design of new biobased additives for industrial formulations.Frontiers in chemistry · 2023Article
- Mechanochemical and Size Reduction Machines for Biorefining.Molecules (Basel, Switzerland) · 2020Review
- Mechanochemical amorphization of chitin: impact of apparatus material on performance and contamination.Beilstein journal of organic chemistry · 2019Article
- Mechanochemistry of nucleosides, nucleotides and related materials.Beilstein journal of organic chemistry · 2018Review
- From beech wood to itaconic acid: case study on biorefinery process integration.Biotechnology for biofuels · 2018Review
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A lipase-catalyzed esterification of lignin model compounds in the ball mill was developed combining the advantages of enzyme catalysis and mechanochemistry. Under the described conditions, the primary aliphatic hydroxy groups present in the substrates were selectively modified by the biocatalyst to afford monoesterified products. Amongst the tested lipases, CALB proved to be the most effective biocatalyst for these transformations. Noteworthy, various acyl donors of different chain lengths were tolerated under the mechanochemical conditions.
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Registered trials
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