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Efficient transesterification of sucrose catalysed by the metalloprotease thermolysin in dimethylsulfoxide
Author(s) -
Pedersen Ninfa Rangel,
Halling Peter J,
Pedersen Lars Haastrup,
Wimmer Reinhard,
Matthiesen Rune,
Veltman Oene Robert
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02753-9
Subject(s) - thermolysin , chemistry , transesterification , proteases , racemization , enzyme , biochemistry , sucrose , organic chemistry , stereochemistry , catalysis , trypsin
Thermolysin catalyses the formation of sucrose esters from sucrose and vinyl laurate in dimethylsulfoxide, with a specific activity of 53 nmol/min/mg and 2‐ O ‐lauroyl‐sucrose as the main product. Such transesterification reactions are normally observed only when the mechanism involves an acyl enzyme intermediate, as with lipases or serine proteases, and not with metalloproteases like thermolysin. A possible reason is the affinity of the active site of thermolysin for sugar moieties, as for the potent inhibitor phosphoramidon. The reaction is not catalysed by other proteins under the same conditions, and is inhibited by removal of the active site zinc.