Appearance and distribution of regioisomers in metallo- and serine-protease-catalysed acylation of sucrose in N,N-dimethylformamide

Aleksander Lie, Anne S. Meyer, Lars Haastrup Pedersen

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Abstract

The appearance and distribution of monoester regioisomers were investigated in the virtually irreversible acylation of sucrose with the enol ester, vinyl laurate, as acyl donor catalysed by serine proteases and a metalloprotease in the hydrophilic, aprotic solvent N,N-dimethylformamide. Sucrose laurate was obtained in yields from 12 to 53% after 48 h under different catalytic conditions. The serine protease ALP-901, derived from a Streptomyces sp., produced the highest yield at this reaction time, while reaction with the zinc-protease thermolysin achieved the overall highest yield (63%) after 6 h, with only monoesters synthesised. The total conversion of sucrose after 48 h ranged from 19 to 96%. The highest degree of conversion was observed in the reaction with thermolysin, while the reactions without protein and with ALP-901 resulted in 82% and 66% sucrose conversion, respectively. 2-O-Lauroyl sucrose was the most abundant monoester regioisomer synthesised and the highest concentration observed was 23.7 mM after 24 h in the thermolysin-catalysed reaction. The highest concentration of 2-O-lauroyl sucrose detected in the reaction catalysed by ALP-901 was 19.0 mM, while it was 17.0 mM in the reaction without protein, both after 48 h. The detected appearance of the sucrose laurate regioisomers largely corresponded to the apparent rates of formation, and 2-O-lauroyl sucrose was among the first regioisomers to appear in all reactions. The observed sucrose laurate regioisomeric distribution after 48 h (2:3:4:6:1:3) was 72:5:2:1:7:14 in the reaction catalysed by ALP-901, and 74:5:2:1:7:13 in the reaction without protein. In the reaction catalysed by thermolysin the distribution was 71:5:2:–:9:13 after 6 h and 86:8:–:–:4:3 after 48 h of reaction. The esterification of sucrose with vinyl laurate without protein in the reaction mixture appeared to be catalysed in the presence of aluminosilicate molecular sieves. Non-catalytic protein in the reaction medium seemed to lower the catalytic activity of the molecular sieves.
Original languageEnglish
JournalJournal of Molecular Catalysis B: Enzymatic
Volume106
Pages (from-to)26-31
Number of pages6
ISSN1381-1177
DOIs
Publication statusPublished - 2014

Keywords

  • Sucrose fatty acid ester
  • Regioisomeric distribution
  • Protease-catalysed acylation
  • Hydrophilic solvent
  • Non-enzymatic catalysis

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