TY - JOUR
T1 - Effect of condensed tannins from tropical legumes on the activity of fibrolytic enzymes from the rumen fungus Neocallimastyx hurleyensis
AU - Sanchez, S.
AU - Lascano, Carlos E.
AU - Owen, E.
AU - Barahona, Rolando
AU - Morris, Phillip
AU - Theodorou, Michael K.
N1 - Barahona, R., Sanchez, S., Lascano, C. E., Owen, E., Morris, P., Theodorou, M. K. (2006). Effect of condensed tannins from tropical legumes on the activity of fibrolytic enzymes from the rumen fungus Neocallimastyx hurleyensis. Enzyme and Microbial Technology, 39, (2), 281-288.
PY - 2006/6/26
Y1 - 2006/6/26
N2 - study was conducted to assess the effect of condensed tannins on the activity of fibrolytic enzymes from the anaerobic rumen fungus, Neocallimastix hurleyensis and a recombinant ferulic acid esterase (FAE) from the aerobic fungus Aspergillus niger. Condensed tannins were extracted from the tropical legumes Desmodium ovalifolium, Flemingia macrophylla, Leucaena leucocephala, Leucaena pallida, Calliandra calothyrsus and Clitoria fairchildiana and incubated in fungal enzyme mixtures or with the recombinant FAE. In most cases, the greatest reductions in enzyme activities were observed with tannins purified from D. ovalifolium and F. macrophylla and the least with tannins from L. leucocephala. Thus, whereas 40 μg ml−1 of condensed tannins from C. calothyrsus and L. leucocephala were needed to halve the activity of N. hurleyensis carboxymethylcellulase (CMCase), just 5.5 μg ml−1 of the same tannins were required to inhibit 50% of xylanase activity. The β-d-glucosidase and β-d-xylosidase enzymes were less sensitive to tannin inhibition and concentrations greater than 100 μg ml−1 were required to reduce their activity by 50%. In other assays, the inhibitory effect of condensed tannins when added to incubation mixtures containing particulate substrates (the primary cell walls of F. arundinacea) or when bound to these substrate was compared. Substrate-associated tannins were more effective in preventing fibrolytic activities than tannins added directly to incubations solutions. It was concluded that condensed tannins from tropical legumes can inhibit fibrolytic enzyme activities, although the extent of the effect was dependent on the tannin, the nature of its association with the substrate and the enzyme involved.
AB - study was conducted to assess the effect of condensed tannins on the activity of fibrolytic enzymes from the anaerobic rumen fungus, Neocallimastix hurleyensis and a recombinant ferulic acid esterase (FAE) from the aerobic fungus Aspergillus niger. Condensed tannins were extracted from the tropical legumes Desmodium ovalifolium, Flemingia macrophylla, Leucaena leucocephala, Leucaena pallida, Calliandra calothyrsus and Clitoria fairchildiana and incubated in fungal enzyme mixtures or with the recombinant FAE. In most cases, the greatest reductions in enzyme activities were observed with tannins purified from D. ovalifolium and F. macrophylla and the least with tannins from L. leucocephala. Thus, whereas 40 μg ml−1 of condensed tannins from C. calothyrsus and L. leucocephala were needed to halve the activity of N. hurleyensis carboxymethylcellulase (CMCase), just 5.5 μg ml−1 of the same tannins were required to inhibit 50% of xylanase activity. The β-d-glucosidase and β-d-xylosidase enzymes were less sensitive to tannin inhibition and concentrations greater than 100 μg ml−1 were required to reduce their activity by 50%. In other assays, the inhibitory effect of condensed tannins when added to incubation mixtures containing particulate substrates (the primary cell walls of F. arundinacea) or when bound to these substrate was compared. Substrate-associated tannins were more effective in preventing fibrolytic activities than tannins added directly to incubations solutions. It was concluded that condensed tannins from tropical legumes can inhibit fibrolytic enzyme activities, although the extent of the effect was dependent on the tannin, the nature of its association with the substrate and the enzyme involved.
U2 - 10.1016/j.enzmictec.2005.10.011
DO - 10.1016/j.enzmictec.2005.10.011
M3 - Article
SN - 1879-0909
VL - 39
SP - 281
EP - 288
JO - Enzyme and Microbial Technology
JF - Enzyme and Microbial Technology
IS - 2
ER -