TY - JOUR
T1 - Characterization of a novel xylanase from Armillaria gemina and its immobilization onto SiO2 nanoparticles
AU - Dhiman, Saurabh Sudha
AU - Kalyani, Dayanand
AU - Jagtap, Sujit Sadashiv
AU - Haw, Jung Rim
AU - Kang, Yun Chan
AU - Lee, Jung Kul
N1 - Funding Information:
Acknowledgments This research was supported by the Converging Research Center Program through the National Research Foundation of Korea, funded by the Ministry of Education, Science and Technology (grant 2011–50210). This study was also supported by Brain Pool 2011 of Konkuk University, Republic of Korea.
PY - 2013/2
Y1 - 2013/2
N2 - Enhanced catalytic activities of different lignocellulases were obtained from Armillaria gemina under statistically optimized parameters using a jar fermenter. This strain showed maximum xylanase, endoglucanase, cellobiohydrolase, and β-glucosidase activities of 1,270, 146, 34, and 15 U mL-1, respectively. Purified A. gemina xylanase (AgXyl) has the highest catalytic efficiency (k cat/K m = 1,440 mg mL -1 s-1) ever reported for any fungal xylanase, highlighting the significance of the current study. We covalently immobilized the crude xylanase preparation onto functionalized silicon oxide nanoparticles, achieving 117 % immobilization efficiency. Further immobilization caused a shift in the optimal pH and temperature, along with a fourfold improvement in the half-life of crude AgXyl. Immobilized AgXyl gave 37.8 % higher production of xylooligosaccharides compared to free enzyme. After 17 cycles, the immobilized enzyme retained 92 % of the original activity, demonstrating its potential for the synthesis of xylooligosaccharides in industrial applications.
AB - Enhanced catalytic activities of different lignocellulases were obtained from Armillaria gemina under statistically optimized parameters using a jar fermenter. This strain showed maximum xylanase, endoglucanase, cellobiohydrolase, and β-glucosidase activities of 1,270, 146, 34, and 15 U mL-1, respectively. Purified A. gemina xylanase (AgXyl) has the highest catalytic efficiency (k cat/K m = 1,440 mg mL -1 s-1) ever reported for any fungal xylanase, highlighting the significance of the current study. We covalently immobilized the crude xylanase preparation onto functionalized silicon oxide nanoparticles, achieving 117 % immobilization efficiency. Further immobilization caused a shift in the optimal pH and temperature, along with a fourfold improvement in the half-life of crude AgXyl. Immobilized AgXyl gave 37.8 % higher production of xylooligosaccharides compared to free enzyme. After 17 cycles, the immobilized enzyme retained 92 % of the original activity, demonstrating its potential for the synthesis of xylooligosaccharides in industrial applications.
KW - Denaturation constant
KW - Enthalpy
KW - Immobilization
KW - SiO
KW - Xylanase
KW - Xylooligosaccharide
UR - http://www.scopus.com/inward/record.url?scp=84874104907&partnerID=8YFLogxK
U2 - 10.1007/s00253-012-4381-9
DO - 10.1007/s00253-012-4381-9
M3 - Article
C2 - 22955325
AN - SCOPUS:84874104907
SN - 0175-7598
VL - 97
SP - 1081
EP - 1091
JO - Applied Microbiology and Biotechnology
JF - Applied Microbiology and Biotechnology
IS - 3
ER -