Uchida_2003_FEMS.Microbiol.Lett_223_123

Reference

Title : Purification and properties of an esterase from Aspergillus nomius HS-1 degrading ethylene glycol dibenzoate - Uchida_2003_FEMS.Microbiol.Lett_223_123
Author(s) : Uchida H , Kurakata Y , Sawamura H , Inamura N , Kotani T , Uwajima T
Ref : FEMS Microbiology Letters , 223 :123 , 2003
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.

PubMedSearch : Uchida_2003_FEMS.Microbiol.Lett_223_123
PubMedID: 12799010

Related information

Substrate BEB

Citations formats

Uchida H, Kurakata Y, Sawamura H, Inamura N, Kotani T, Uwajima T (2003)
Purification and properties of an esterase from Aspergillus nomius HS-1 degrading ethylene glycol dibenzoate
FEMS Microbiology Letters 223 :123

Uchida H, Kurakata Y, Sawamura H, Inamura N, Kotani T, Uwajima T (2003)
FEMS Microbiology Letters 223 :123