ISSN:
0006-3592
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bit.260250404
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