TY - JOUR
T1 - Study of the intracellular xylanolytic activity of the phytopathogenic fungus Sporisorium reilianum
AU - Pérez-Rodríguez, Joany
AU - Téllez-Jurado, Alejandro
AU - Álvarez-Cervantes, Jorge
AU - Antonio Ibarra, J.
AU - Jaramillo-Loranca, Blanca Estela
AU - Anducho-Reyes, Miguel Angel
AU - Mercado-Flores, Yuridia
N1 - Publisher Copyright:
© 2019 The Mycological Society of Japan
PY - 2020/3
Y1 - 2020/3
N2 - The present study demonstrates that Sporisorium reilianum, a phytopathogenic fungus of corn, produces intracellular xylanolytic activity during submerged fermentation. Production reached its highest levels in a medium containing glucose, corn hemicellulose and yeast extract. An intracellular xylanase was purified by a process that included precipitation with ammonium sulfate, ion exchange chromatography and gel filtration. Optimal pH and temperature values were 5.0 and 60 °C, respectively. The enzyme showed activity through a broad pH range. The molecular weights of pure xylanase were 36 and 37 kDa, determined by SDS PAGE and gel filtration, respectively. Km and Vmax were 0.160 mg/mL and 1.564 μmol/min/mg, respectively, on a substrate of birchwood xylan. SDS, EDTA, β-Mercaptoethanol, Tween 80, Triton and Mn2+ and Ca2+ strongly inhibited activity. The purified enzyme hydrolyzed xylan, releasing xylotriose and xylobiose. Sequence protein analysis showed 95% similarity with the theoretical protein encoded by the sr14403 gene of S. reilianum, which encodes a putative endo-β-1,4-xylanase. The enzyme is an isoform of the extracellular xylanase SRXL1 of this basidiomycete.
AB - The present study demonstrates that Sporisorium reilianum, a phytopathogenic fungus of corn, produces intracellular xylanolytic activity during submerged fermentation. Production reached its highest levels in a medium containing glucose, corn hemicellulose and yeast extract. An intracellular xylanase was purified by a process that included precipitation with ammonium sulfate, ion exchange chromatography and gel filtration. Optimal pH and temperature values were 5.0 and 60 °C, respectively. The enzyme showed activity through a broad pH range. The molecular weights of pure xylanase were 36 and 37 kDa, determined by SDS PAGE and gel filtration, respectively. Km and Vmax were 0.160 mg/mL and 1.564 μmol/min/mg, respectively, on a substrate of birchwood xylan. SDS, EDTA, β-Mercaptoethanol, Tween 80, Triton and Mn2+ and Ca2+ strongly inhibited activity. The purified enzyme hydrolyzed xylan, releasing xylotriose and xylobiose. Sequence protein analysis showed 95% similarity with the theoretical protein encoded by the sr14403 gene of S. reilianum, which encodes a putative endo-β-1,4-xylanase. The enzyme is an isoform of the extracellular xylanase SRXL1 of this basidiomycete.
KW - Head smut
KW - Xylan degradation
KW - Xylanase
UR - http://www.scopus.com/inward/record.url?scp=85075504848&partnerID=8YFLogxK
U2 - 10.1016/j.myc.2019.10.005
DO - 10.1016/j.myc.2019.10.005
M3 - Artículo
AN - SCOPUS:85075504848
SN - 1340-3540
VL - 61
SP - 76
EP - 84
JO - Mycoscience
JF - Mycoscience
IS - 2
ER -