Purification and properties of an esterase from Aspergillus nomius HS-1 degrading ethylene glycol dibenzoate.

Abstract:

:We isolated a fungal strain HS-1 utilizing either ethylene glycol dibenzoate or ethyl benzoate as sole source of carbon and energy, and identified it as Aspergillus nomius, based on morphological and rDNA analyses. An enzyme hydrolyzing the esters was purified from the culture supernatant of the strain to an electrophoretically homogeneous state. The enzyme was a carboxyl esterase with a monomeric structure, of which the molecular mass was about 60000, and inhibited by phenylmethylsulfonyl fluoride. The enzyme hydrolyzed various benzoate esters and p-nitrophenyl esters, and its hydrolysis rates for the most favorable substrates, n-butyl benzoate and p-nitrophenyl valerate, were comparable.

journal_name

FEMS Microbiol Lett

authors

Uchida H,Kurakata Y,Sawamura H,Inamura N,Kotani T,Uwajima T

doi

10.1016/S0378-1097(03)00353-7

keywords:

subject

Has Abstract

pub_date

2003-06-06 00:00:00

pages

123-7

issue

1

eissn

0378-1097

issn

1574-6968

pii

S0378109703003537

journal_volume

223

pub_type

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