ReviewApplied microbiology and biotechnology2017
Comparison of lipases and glycoside hydrolases as catalysts in synthesis reactions.
Review in Applied microbiology and biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 30 citations in OpenAlex.
- The P134Q Sucrose Phosphorylase: Subtle Changes in the Catalytic Properties Benefit the Production of 2-O-α-Glucosyl Glycerol.Biotechnology and bioengineering · 2025Article
- Flavonoids as Aglycones in Retaining Glycosidase-Catalyzed Reactions: Prospects for Green Chemistry.Journal of agricultural and food chemistry · 2023Review
- Xylitol as a Hydrophilization Moiety for a Biocatalytically Synthesized Ibuprofen Prodrug.International journal of molecular sciences · 2022Article
- Three-level hybrid modeling for systematic optimization of biocatalytic synthesis: α-glucosyl glycerol production by enzymatic trans-glycosylation from sucrose.Biotechnology and bioengineering · 2021Article
- Biocatalytic Approach for Direct Esterification of Ibuprofen with Sorbitol in Biphasic Media.International journal of molecular sciences · 2021Article
- An Integrated Enzymatic Approach to Produce Pentyl Xylosides and Glucose/Xylose Laurate Esters From Wheat Bran.Frontiers in bioengineering and biotechnology · 2021Article
- On the donor substrate dependence of group-transfer reactions by hydrolytic enzymes: Insight from kinetic analysis of sucrose phosphorylase-catalyzed transglycosylation.Biotechnology and bioengineering · 2020Article
- β-Mannanase-catalyzed synthesis of alkyl mannooligosides.Applied microbiology and biotechnology · 2018Article
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Abstract
Lipases and glycoside hydrolases have large similarities concerning reaction mechanisms. Acyl-enzyme intermediates are formed during lipase-catalyzed reactions and in an analogous way, retaining glycoside hydrolases form glycosyl-enzyme intermediates during catalysis. In both cases, the covalent enzyme intermediates can react with water or other nucleophiles containing hydroxyl groups. Simple alcohols are accepted as nucleophiles by both types of enzymes. Lipases are used very successfully in synthesis applications due to their efficiency in catalyzing reversed hydrolysis and transesterification reactions. On the other hand, synthesis applications of glycoside hydrolases are much less developed. Here, important similarities and differences between the enzyme groups are reviewed and approaches to reach high synthesis yields are discussed. Useful strategies include the use of low-water media, high nucleophile concentrations, as well as protein engineering to modify the selectivity of the enzymes. The transglycosylases, hydrolases which naturally catalyze mainly transfer reactions, are of special interest and might be useful guides for engineering of other hydrolases.
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