TY - JOUR
T1 - Synergistic degradation of arabinoxylan by free and immobilized xylanases and arabinofuranosidase
AU - Jia, Lili
AU - Budinova, Geisa A.L.G.
AU - Takasugi, Yusaku
AU - Noda, Shuhei
AU - Tanaka, Tsutomu
AU - Ichinose, Hirofumi
AU - Goto, Masahiro
AU - Kamiya, Noriho
N1 - Funding Information:
This research was supported by the Advanced Low Carbon Technology Research and Development Program (ALCA) from the Japan Science and Technology Agency (JST) and in part by the Japan Society for the Promotion of Science (JSPS) KAKENHI (No. 16H04581 ). L. Jia thanks the China Scholarship Council (grant number: 201306300044 ).
Publisher Copyright:
© 2016 Elsevier B.V.
PY - 2016/10/15
Y1 - 2016/10/15
N2 - Effective degradation of hemicellulose is of utmost importance in a wide variety of applications in bioindustry. Five endoxylanases from different glycoside hydrolase families and microorganisms were tested with an arabinofuranosidase, Araf51A, for the hydrolysis of insoluble wheat arabinoxylan, which is a structural component of hemicellulose. The optimized combination was XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increased with the increase of Araf51A proportion in the enzyme mixture. Afterwards, selected enzymes were immobilized on commercial magnetic nanoparticles through covalent bonding. Both free and immobilized enzymes showed a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes was retained. A 5.5-fold increase in the production of sugars was obtained with a mixture of enzymes immobilized after 10 cycles in total compared with free enzymes. Importantly, a sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan was demonstrated.
AB - Effective degradation of hemicellulose is of utmost importance in a wide variety of applications in bioindustry. Five endoxylanases from different glycoside hydrolase families and microorganisms were tested with an arabinofuranosidase, Araf51A, for the hydrolysis of insoluble wheat arabinoxylan, which is a structural component of hemicellulose. The optimized combination was XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increased with the increase of Araf51A proportion in the enzyme mixture. Afterwards, selected enzymes were immobilized on commercial magnetic nanoparticles through covalent bonding. Both free and immobilized enzymes showed a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes was retained. A 5.5-fold increase in the production of sugars was obtained with a mixture of enzymes immobilized after 10 cycles in total compared with free enzymes. Importantly, a sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan was demonstrated.
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U2 - 10.1016/j.bej.2016.07.013
DO - 10.1016/j.bej.2016.07.013
M3 - Article
AN - SCOPUS:84979737548
SN - 1369-703X
VL - 114
SP - 268
EP - 275
JO - Biochemical Engineering Journal
JF - Biochemical Engineering Journal
ER -