TY - JOUR
T1 - Effect of pretreatment methods on the synergism of cellulase and xylanase during the hydrolysis of bagasse
AU - Jia, Lili
AU - Gonçalves, Geisa A.L.
AU - Takasugi, Yusaku
AU - Mori, Yutaro
AU - Noda, Shuhei
AU - Tanaka, Tsutomu
AU - Ichinose, Hirofumi
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) . L. Jia thanks the China Scholarship Council (Grant Number: 201306300044 ).
Publisher Copyright:
© 2015 Elsevier Ltd.
PY - 2015/6/1
Y1 - 2015/6/1
N2 - The effect of pretreatment with peracetic acid (PAA) or an ionic liquid (1-ethyl-3-methylimidazolium acetate, [Emim][OAc]) on the synergism between endoglucanase and endoxylanase in the hydrolysis of bagasse was investigated. An endoglucanase, Cel6A, with a carbohydrate-binding module (CBM) and two endoxylanases, XynZ-C without a CBM and Xyn11A with an intrinsic xylan/cellulose binding module (XBM), were selected. The hemicellulose content, especially arabinan, and the cellulose crystallinity of bagasse were found to affect the cellulase-xylanase synergism. More specifically, higher synergism (above 3.4) was observed for glucan conversion, at low levels of arabinan (0.9%), during the hydrolysis of PAA pretreated bagasse. In contrast, [Emim][OAc] pretreated bagasse, showed lower cellulose crystallinity and achieved higher synergism (over 1.9) for xylan conversion. Ultimately, the combination of Cel6A and Xyn11A resulted in higher synergism for glucan conversion than the combination of Cel6A with XynZ-C, indicating the importance of the molecular architecture of enzymes for metabolic synergism.
AB - The effect of pretreatment with peracetic acid (PAA) or an ionic liquid (1-ethyl-3-methylimidazolium acetate, [Emim][OAc]) on the synergism between endoglucanase and endoxylanase in the hydrolysis of bagasse was investigated. An endoglucanase, Cel6A, with a carbohydrate-binding module (CBM) and two endoxylanases, XynZ-C without a CBM and Xyn11A with an intrinsic xylan/cellulose binding module (XBM), were selected. The hemicellulose content, especially arabinan, and the cellulose crystallinity of bagasse were found to affect the cellulase-xylanase synergism. More specifically, higher synergism (above 3.4) was observed for glucan conversion, at low levels of arabinan (0.9%), during the hydrolysis of PAA pretreated bagasse. In contrast, [Emim][OAc] pretreated bagasse, showed lower cellulose crystallinity and achieved higher synergism (over 1.9) for xylan conversion. Ultimately, the combination of Cel6A and Xyn11A resulted in higher synergism for glucan conversion than the combination of Cel6A with XynZ-C, indicating the importance of the molecular architecture of enzymes for metabolic synergism.
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U2 - 10.1016/j.biortech.2015.02.041
DO - 10.1016/j.biortech.2015.02.041
M3 - Article
C2 - 25768418
AN - SCOPUS:84924347656
SN - 0960-8524
VL - 185
SP - 158
EP - 164
JO - Agricultural Wastes
JF - Agricultural Wastes
ER -
