Open AccessCloning of a gene encoding cinnamoyl ester hydrolase from the ruminai bacterium Butyrivibrio fibrisolvens E14 by a novel method
Author(s) -
Dalrymple Brian P.,
Swadling Yolande,
Cybinski Daisy H.,
Xue GangPing
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08469.x
Subject(s) - catalytic triad , biochemistry , serine hydrolase , pseudomonas fluorescens , histidine , amino acid , ferulic acid , esterase , chemistry , clostridium thermocellum , periplasmic space , biology , bacteria , serine , peptide sequence , gene , escherichia coli , enzyme , genetics , cellulase
A gene ( cin I) encoding a cinnamoyl ester hydrolase (CEH) has been isolated from the ruminai bacterium, Butyrivibrio fibrisohens E14, using a model substrate, MUTMAC [4‐methylumbelliferoyl ( p ‐trimethylammonium cinnamate chloride)]. CinI has significant amino‐acid similarities with members of a large and diverse family of hydrolases with a serine/aspartic acid/ histidine catalytic triad. Our analyses identified two previously unclassified amino acid sequences, the amino‐terminal domain of unknown function in XynZ from Clostridium thermocellum and XynC, an acetylxylan esterase from Caldicellulosiruptor saccharolyticus , as members of the same family of hydrolases. A previously described esterase with CEH activity, XylD from Pseudomonas fluorescens ssp. cellulosa , is not similar to CinI. CinI was expressed at high levels in the periplasmic fraction of E. coli TOPP2 and released ferulic acid from Fara [5‐ O ‐( trans ‐feruloyl)‐arabinofuranose] prepared from wheat bran.