Ensiling alfalfa and alfalfa–bermudagrass with ferulic acid esterase‐producing microbial inoculants

cftm ◽  
2021 ◽  
Author(s):  
Taylor J. Hendricks ◽  
Dennis W. Hancock ◽  
Jennifer J. Tucker ◽  
Fabio J. Maia ◽  
Jeferson M. Lourenco
Keyword(s):  
Ferulic Acid ◽  
Ferulic Acid Esterase ◽  
Microbial Inoculants

Production and biochemical characterization of a type B ferulic acid esterase from Streptomyces ambofaciens

2009 ◽  
Vol 55 (6) ◽  
pp. 729-738 ◽  
Author(s):  
Fadi Kheder ◽  
Stéphane Delaunay ◽  
Ghassan Abo-Chameh ◽  
Cédric Paris ◽  
Lionel Muniglia ◽  
...  
Keyword(s):  
Ferulic Acid ◽  
Wheat Bran ◽  
Biochemical Characterization ◽  
Extracellular Enzyme ◽  
Type B ◽  
Ferulic Acid Esterase ◽  
Level Of Activity ◽  
Streptomyces Ambofaciens ◽  
Methyl Ferulate ◽  
First Time

For the first time, the presence of a ferulic acid esterase (FAE) was demonstrated in Streptomyces ambofaciens . This extracellular enzyme was produced on a range of lignocellulosic substrates. The maximal level of activity was detected in the presence of either destarched wheat bran or oat spelt xylan as the sole carbon source. We found that 1% (m/v) of destarched wheat bran was the optimal concentration to induce its production. With this inducer, no ferulic acid dimers were released from the cell wall by the produced FAE. Interestingly, rape cattle cake ( Brassica napus ), which does not contain esterified ferulic acid, was also shown to induce the production of the FAE from S. ambofaciens. The FAE was partially purified from the culture supernatant. The purified enzyme was optimally active at pH 7 and 40 °C. The substrate specificity of the FAE from S. ambofaciens was investigated: the highest activity was determined with methyl p-coumarate, methyl ferulate, and methyl cinnamate. Furthermore, the FAE required a certain distance between the benzene ring and the ester bond to be active. According to these biochemical characteristics, the FAE from S. ambofaciens has been classified as a type B FAE.

scholarly journals Biochemical Analysis of a β-d-Xylosidase and a Bifunctional Xylanase-Ferulic Acid Esterase from a Xylanolytic Gene Cluster in Prevotella ruminicola 23

2009 ◽  
Vol 191 (10) ◽  
pp. 3328-3338 ◽  
Author(s):  
Dylan Dodd ◽  
Svetlana A. Kocherginskaya ◽  
M. Ashley Spies ◽  
Kyle E. Beery ◽  
Charles A. Abbas ◽  
...  
Keyword(s):  
Recombinant Protein ◽  
Ferulic Acid ◽  
Biochemical Analysis ◽  
Directed Mutagenesis ◽  
Ferulic Acid Esterase ◽  
Prevotella Ruminicola ◽  
Obligate Anaerobic ◽  
Catalytic Sites ◽  
Cellular Machinery ◽  
Biochemical Analyses

ABSTRACT Prevotella ruminicola 23 is an obligate anaerobic bacterium in the phylum Bacteroidetes that contributes to hemicellulose utilization within the bovine rumen. To gain insight into the cellular machinery that this organism elaborates to degrade the hemicellulosic polymer xylan, we identified and cloned a gene predicted to encode a bifunctional xylanase-ferulic acid esterase (xyn10D-fae1A) and expressed the recombinant protein in Escherichia coli. Biochemical analysis of purified Xyn10D-Fae1A revealed that this protein possesses both endo-β-1,4-xylanase and ferulic acid esterase activities. A putative glycoside hydrolase (GH) family 3 β-d-glucosidase gene, with a novel PA14-like insertion sequence, was identified two genes downstream of xyn10D-fae1A. Biochemical analyses of the purified recombinant protein revealed that the putative β-d-glucosidase has activity for pNP-β-d-xylopyranoside, pNP-α-l-arabinofuranoside, and xylo-oligosaccharides; thus, the gene was designated xyl3A. When incubated in combination with Xyn10D-Fae1A, Xyl3A improved the release of xylose monomers from a hemicellulosic xylan substrate, suggesting that these two enzymes function synergistically to depolymerize xylan. Directed mutagenesis studies of Xyn10D-Fae1A mapped the catalytic sites for the two enzymatic functionalities to distinct regions within the polypeptide sequence. When a mutation was introduced into the putative catalytic site for the xylanase domain (E280S), the ferulic acid esterase activity increased threefold, which suggests that the two catalytic domains for Xyn10D-Fae1A are functionally coupled. Directed mutagenesis of conserved residues for Xyl3A resulted in attenuation of activity, which supports the assignment of Xyl3A as a GH family 3 β-d-xylosidase.

Fiber degradability, chemical composition and conservation characteristics of alfalfa haylage ensiled with exogenous fibrolytic enzymes and a ferulic acid esterase-producing inoculant

2014 ◽  
Vol 94 (4) ◽  
pp. 697-704 ◽  
Author(s):  
J. P. Lynch ◽  
D. Prema ◽  
J. D. Van Hamme ◽  
J. S. Church ◽  
K. A. Beauchemin
Keyword(s):  
Chemical Composition ◽  
Ferulic Acid ◽  
Untreated Control ◽  
Dry Matter ◽  
Neutral Detergent Fiber ◽  
Ferulic Acid Esterase ◽  
Acid Detergent Fiber ◽  
Fibrolytic Enzymes ◽  
Effect Of Treatment

Lynch, J. P., Prema, D., Van Hamme, J. D., Church, J. S. and Beauchemin, K. A. 2014. Fiber degradability, chemical composition and conservation characteristics of alfalfa haylage ensiled with exogenous fibrolytic enzymes and a ferulic acid esterase-producing inoculant. Can. J. Anim. Sci. 94: 697–704. This study investigated the effects of two fibrolytic enzyme products, applied at baling alone or in combination with a ferulic acid esterase-producing bacterial additive, on the ensilage dynamics, chemical composition and digestibility of alfalfa haylage. Five replicate wrapped bales were produced with one of five treatments, including an untreated control, and one of two fibrolytic enzyme products (EN1 and EN2) applied either alone or in combination with a ferulic-acid producing bacterial additive (FAEI). No effect of treatment was observed on the neutral detergent fiber (NDF) (P=0.889) or acid detergent fiber (ADF) (P=0.065) concentrations of haylage after ensilage, but haylage produced using fibrolytic enzyme products underwent greater (P<0.018) increases in temperature following exposure to aerobic conditions. Haylages produced with fibrolytic enzyme products had a greater (P<0.001) in vitro NDF degradability (NDFD) than untreated haylage. The use of fibrolytic enzymes applied to alfalfa haylage at ensiling increased the NDFD, despite minimal effects on the chemical composition of the herbage. However, the greater aerobic deterioration of fibrolytic enzyme-treated bales indicates higher dry matter losses during aerobic exposure. The use of FAEI with fibrolytic enzymes did not further enhance the effects of fibrolytic-enzyme treatments.

Studies on ferulic acid esterase activity in fungal lipases and cutinases

2002 ◽  
Vol 26 (1-2) ◽  
pp. 47-55 ◽  
Author(s):  
A Andersen ◽  
A Svendsen ◽  
J Vind ◽  
S.F Lassen ◽  
C Hjort ◽  
...  
Keyword(s):  
Ferulic Acid ◽  
Esterase Activity ◽  
Ferulic Acid Esterase

scholarly journals Generation of transgenic wheat (Triticum aestivumL.) accumulating heterologous endo-xylanase or ferulic acid esterase in the endosperm

2010 ◽  
Vol 8 (3) ◽  
pp. 351-362 ◽  
Author(s):  
Jesper Harholt ◽  
Inga C. Bach ◽  
Solveig Lind-Bouquin ◽  
Kylie J. Nunan ◽  
Susan M. Madrid ◽  
...  
Keyword(s):  
Ferulic Acid ◽  
Transgenic Wheat ◽  
Ferulic Acid Esterase

Functional co-expression of a fungal ferulic acid esterase and a β-1,4 endoxylanase in Festuca arundinacea (tall fescue) modifies post-harvest cell wall deconstruction

Planta ◽  
2015 ◽  
Vol 242 (1) ◽  
pp. 97-111 ◽  
Author(s):  
Marcia M. de O. Buanafina ◽  
Sue Dalton ◽  
Tim Langdon ◽  
E. Timms-Taravella ◽  
Erica A. Shearer ◽  
...  
Keyword(s):  
Cell Wall ◽  
Ferulic Acid ◽  
Tall Fescue ◽  
Festuca Arundinacea ◽  
Ferulic Acid Esterase ◽  
Post Harvest
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