TY - JOUR
T1 - Effect of the single mutation N9Y on the catalytical properties of xylanase Xyn11A from Cellulomonas uda
T2 - A biochemical and molecular dynamic simulation analysis
AU - Cayetano-Cruz, Maribel
AU - Caro-Gómez, Luis A.
AU - Plascencia-Espinosa, Miguel
AU - Santiago-Hernández, Alejandro
AU - Benítez-Cardoza, Claudia G.
AU - Campos, Jorge E.
AU - Hidalgo-Lara, María Eugenia
AU - Zamorano-Carrillo, Absalom
N1 - Publisher Copyright:
© 2021 The Author(s) 2021. Published by Oxford University Press on behalf of Japan Society for Bioscience, Biotechnology, and Agrochemistry.
PY - 2021/9/1
Y1 - 2021/9/1
N2 - Cellulomonas uda produces Xyn11A, moderately thermostable xylanase, with optimal activity at 50 °C and pH 6.5. An improvement in the biochemical properties of Xyn11A was achieved by site-directed mutagenesis approach. Wild-Type xylanase, Xyn11A-WT, and its mutant Xyn11A-N9Y were expressed in Escherichia coli, and then both enzymes were purified and characterized. Xyn11A-N9Y displayed optimal activity at 60 °C and pH 7.5, an upward shift of 10 °C in the optimum temperature and an upward shift of 1 unit in optimum pH; also, it manifested an 11-fold increase in thermal stability at 60 °C, compared to that displayed by Xyn11A-WT. Molecular dynamics simulations of Xyn11A-WT and Xyn11A-N9Y suggest that the substitution N9Y leads to an array of secondary structure changes at the N-Terminal end and an increase in the number of hydrogen bonds in Xyn11A-N9Y. Based on the significant improvements, Xyn11A-N9Y may be considered as a candidate for several biotechnological applications.
AB - Cellulomonas uda produces Xyn11A, moderately thermostable xylanase, with optimal activity at 50 °C and pH 6.5. An improvement in the biochemical properties of Xyn11A was achieved by site-directed mutagenesis approach. Wild-Type xylanase, Xyn11A-WT, and its mutant Xyn11A-N9Y were expressed in Escherichia coli, and then both enzymes were purified and characterized. Xyn11A-N9Y displayed optimal activity at 60 °C and pH 7.5, an upward shift of 10 °C in the optimum temperature and an upward shift of 1 unit in optimum pH; also, it manifested an 11-fold increase in thermal stability at 60 °C, compared to that displayed by Xyn11A-WT. Molecular dynamics simulations of Xyn11A-WT and Xyn11A-N9Y suggest that the substitution N9Y leads to an array of secondary structure changes at the N-Terminal end and an increase in the number of hydrogen bonds in Xyn11A-N9Y. Based on the significant improvements, Xyn11A-N9Y may be considered as a candidate for several biotechnological applications.
KW - 1,4-β-endo-xylanase
KW - aromatic-Aromatic interaction
KW - hydrogen bonds
KW - molecular dynamics simulations
KW - thermal stability
UR - http://www.scopus.com/inward/record.url?scp=85114751499&partnerID=8YFLogxK
U2 - 10.1093/bbb/zbab124
DO - 10.1093/bbb/zbab124
M3 - Artículo
C2 - 34232281
AN - SCOPUS:85114751499
SN - 0916-8451
VL - 85
SP - 1971
EP - 1985
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
IS - 9
ER -