TY - JOUR
T1 - The thermophilic biomass-degrading fungus Thielavia terrestris Co3Bag1 produces a hyperthermophilic and thermostable β-1,4-xylanase with exo- and endo-activity
AU - García-Huante, Yolanda
AU - Cayetano-Cruz, Maribel
AU - Santiago-Hernández, Alejandro
AU - Cano-Ramírez, Claudia
AU - Marsch-Moreno, Rodolfo
AU - Campos, Jorge E.
AU - Aguilar-Osorio, Guillermo
AU - Benitez-Cardoza, Claudia G.
AU - Trejo-Estrada, Sergio
AU - Hidalgo-Lara, María Eugenia
N1 - Publisher Copyright:
© 2016, Springer Japan.
PY - 2017/1/1
Y1 - 2017/1/1
N2 - A hyperthermophilic and thermostable xylanase of 82 kDa (TtXynA) was purified from the culture supernatant of T. terrestris Co3Bag1, grown on carboxymethyl cellulose (CMC), and characterized biochemically. TtXynA showed optimal xylanolytic activity at pH 5.5 and at 85 °C, and retained more than 90% of its activity at a broad pH range (4.5–10). The enzyme is highly thermostable with a half-life of 23.1 days at 65 °C, and active in the presence of several metal ions. Circular dichroism spectra strongly suggest the enzyme gains secondary structures when temperature increases. TtXynA displayed higher substrate affinity and higher catalytic efficiency towards beechwood xylan than towards birchwood xylan, oat-spelt xylan, and CMC. According to its final hydrolysis products, TtXynA displays endo-/exo-activity, yielded xylobiose, an unknown oligosaccharide containing about five residues of xylose and a small amount of xylose on beechwood xylan. Finally, this report represents the description of the first fungal hyperthermophilic xylanase which is produced by T. terrestris Co3Bag1. Since TtXynA displays relevant biochemical properties, it may be a suitable candidate for biotechnological applications carried out at high temperatures, like the enzymatic pretreatment of plant biomass for the production of bioethanol.
AB - A hyperthermophilic and thermostable xylanase of 82 kDa (TtXynA) was purified from the culture supernatant of T. terrestris Co3Bag1, grown on carboxymethyl cellulose (CMC), and characterized biochemically. TtXynA showed optimal xylanolytic activity at pH 5.5 and at 85 °C, and retained more than 90% of its activity at a broad pH range (4.5–10). The enzyme is highly thermostable with a half-life of 23.1 days at 65 °C, and active in the presence of several metal ions. Circular dichroism spectra strongly suggest the enzyme gains secondary structures when temperature increases. TtXynA displayed higher substrate affinity and higher catalytic efficiency towards beechwood xylan than towards birchwood xylan, oat-spelt xylan, and CMC. According to its final hydrolysis products, TtXynA displays endo-/exo-activity, yielded xylobiose, an unknown oligosaccharide containing about five residues of xylose and a small amount of xylose on beechwood xylan. Finally, this report represents the description of the first fungal hyperthermophilic xylanase which is produced by T. terrestris Co3Bag1. Since TtXynA displays relevant biochemical properties, it may be a suitable candidate for biotechnological applications carried out at high temperatures, like the enzymatic pretreatment of plant biomass for the production of bioethanol.
KW - Circular dichroism
KW - Endo-xylanase/exo-activity
KW - Hyperthermophilic xylanase
KW - Thermophilic fungus
KW - Thermostable xylanase
KW - Thielavia terrestris
UR - http://www.scopus.com/inward/record.url?scp=85000866226&partnerID=8YFLogxK
U2 - 10.1007/s00792-016-0893-z
DO - 10.1007/s00792-016-0893-z
M3 - Artículo
SN - 1431-0651
VL - 21
SP - 175
EP - 186
JO - Extremophiles
JF - Extremophiles
IS - 1
ER -