Title : Cloning and characterization of a bacterial cell-bound type B carboxylesterase from Bacillus sp. BP-7 - Prim_2001_Curr.Microbiol_42_237 |
Author(s) : Prim N , Pastor FI , Diaz P |
Ref : Curr Microbiol , 42 :237 , 2001 |
Abstract :
A clone producing halos on tributyrin plates was isolated from a genomic library of Bacillus sp. BP-7. The insert contained an open reading frame that coded for a protein of 487 amino acids with homology to carboxylesterases. The cloned enzyme showed clear preference for esters of short-chain fatty acids, being classified as an esterase. Maximum activity was found at 45 degrees C and pH 7.5. The enzyme displayed stability in the pH range from 6 to 9.5, and at temperatures from 4 degrees to 45 degrees C. Zymogram analysis of the protein revealed a molecular mass of 53 kDa and a pI of 5.1. The enzyme showed homology to members of the bacterial subclass of type B carboxylesterases, a set of proteins potentially useful for biotechnological applications. |
PubMedSearch : Prim_2001_Curr.Microbiol_42_237 |
PubMedID: 11178722 |
Gene_locus related to this paper: bacsp-este7 |
Gene_locus | bacsp-este7 |
Prim N, Pastor FI, Diaz P (2001)
Cloning and characterization of a bacterial cell-bound type B carboxylesterase from Bacillus sp. BP-7
Curr Microbiol
42 :237
Prim N, Pastor FI, Diaz P (2001)
Curr Microbiol
42 :237