Cloning of a gene encoding cinnamoyl ester hydrolase from the ruminai bacterium Butyrivibrio fibrisolvens E14 by a novel method

Abstract

A gene (cinI) encoding a cinnamoyl ester hydrolase (CEH) has been isolated from the ruminal bacterium, Butyrivibrio fibrisolvens 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.

Thermostable feruloyl esterase for the bioproduction of ferulic acid from triticale bran

“…The 246-residue amino acid sequence of a biochemically characterized cinnamoyl esterase (AAC44493) from B. fibrisolvens (Dalrymple et al 1996) was used to perform a BLAST search of the National Center for Biotechnology Information (NCBI) database. We were interested in a potential thermophilic candidate.…”

“…On the bacterial side, even fewer clones are available. These are limited to Cellvibrio japonicum (DeBoy et al 2008; formerly Pseudomonas fluorescens; Ferreira et al 1993), Burkholderia multivorans (Rashamuse et al 2007), Butyrivibrio fibrisolvens (Dalrymple et al 1996;Dalrymple and Swadling 1997), Pseudoalteromonas halosplanktis (Aurilia et al 2008), Clostridium thermocellum cellulosome (Blum et al 2000), and Prevotella ruminicola (Dodd et al 2009). …”

Purification and Properties of a Feruloyl Esterase Involved in Lignocellulose Degradation byAureobasidium pullulans

“…Several hydroxycinnamic ester-hydrolyzing enzymes have been isolated and characterized (39,40), some have been cloned (2,10,12,16), and three-dimensional structures are now available (29). Extracellular feruloyl esterases are produced by plant-invading microorganisms in addition to other lignocellulose-degrading enzymes but have also been reported to be endogenous to plants, such as in germinating barley (36).…”

Feruloyl Esterase Activity of the Clostridium thermocellum Cellulosome Can Be Attributed to Previously Unknown Domains of XynY and XynZ

“…1) shows that these domains have substantial homology. This homology was not apparent with feruloyl esterases of Aspergillus niger and Aspergillus tubingensis (15), CinA and CinB from Butyrivibrio fibrisolvens (13,14), and XylD from Pseudomonas fluorescens subsp. cellulosa (18).…”