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Preparative separation of α‐ and β‐naphthols catalyzed by immobilized sulfatase
Author(s) -
Pelsy Gilles,
Klibanov Alexander M.
Publication year - 1983
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260250404
Subject(s) - chemistry , hydrolysis , sulfatase , helix pomatia , sulfate , sulfation , benzene , steric effects , chromatography , organic chemistry , enzymatic hydrolysis , aqueous solution , enzyme , phenols , biochemistry , ecology , snail , biology
It has been found that sulfatase from Helix pomatia hydrolyzes β‐naphthyl sulfate much faster than α‐naphthyl sulfate; e.g., at pH 7.8, while the former is readily hydrolyzed, the latter undergoes no appreciable hydrolysis. Kinetic investigations of both enzymatic and acid hydrolysis of naphthyl sulfates and their analogs indicate that in the enzymatic reaction the difference in reactivities is due to steric hindrances exerted in α‐naphthyl sulfate by the benzene ring adjacent to the one bearing the sulfate group. (In the β‐ester this ring is remote from the site of hydrolysis.) The enzyme was immobilized and employed for the preparative resolution of α‐ and β‐naphthols: a mixture of the isomers was first sulfated with chlorosulfonic acid and then incubated with sulfatase covalently attached to alumina. The β‐naphthol produced was extracted with benzene, followed by acid hydrolysis of α‐naphthyl sulfate in the remaining aqueous solution and extraction of the α‐naphthol formed. Helix pomatia sulfatase also expresses a marked regiospecificity in the hydrolysis of ortho and para substituted phenyl sulfates. Therefore, the enzyme can be used for the preparative separation of naphthols as well as a variety of isomeric phenols.