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   <subfield code="a">Promotion of crystalline cellulose degradation by expansins from Oryza sativa</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Yasutaka Seki, Yukiko Kikuchi, Ryo Yoshimoto, Kenichi Aburai, Yoshihiro Kanai, Tatsushi Ruike, Kazuki Iwabata, Ryo Goitsuka, Fumio Sugawara, Masahiko Abe, Kengo Sakaguchi]</subfield>
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   <subfield code="a">Main conclusion : Enzymatic activities of Oryza sativa expansins, which were heterologously overexpressed in Escherichia coli , were analyzed. Results suggested that expansins promote degradation of cellulose by cellulase in a synergistic manner. Abstract: Sustainable production of future biofuels is dependent on efficient saccharification of lignocelluloses. Expansins have received a lot of attention as proteins promoting biological degradation of cellulose using cellulase. The expansins are a class of plant cell wall proteins that induce cell wall loosening without hydrolysis. In this study, the expansins from Oryza sativa were classified using phylogenetic analysis and five proteins were selected for functional evaluation. At low cellulose loading, the cellulase in expansin mixtures was up to 2.4 times more active than in mixtures containing only cellulase, but at high cellulose loading the activity of cellulase in expansin mixtures and cellulase only mixtures did not differ. Furthermore, expansin activity was greater in cellulase mixtures compared with cellulase-deficient mixtures. Therefore, the expansins showed significant synergistic activity with cellulase. Expansin may play an important role in efficient saccharification of cellulose.</subfield>
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   <subfield code="a">Springer-Verlag Berlin Heidelberg, 2014</subfield>
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   <subfield code="a">Cellulase</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">HPLC</subfield>
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   <subfield code="a">X-Ray diffraction</subfield>
   <subfield code="2">nationallicence</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">Pre-reacted experiment</subfield>
   <subfield code="2">nationallicence</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">Addition order experiment</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">Synergistic activity</subfield>
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   <subfield code="u">Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda-shi, 278-8510, Chiba-Ken, Japan</subfield>
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   <subfield code="a">Kikuchi</subfield>
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   <subfield code="u">Department of Industrial Chemistry, Tokyo University of Science, Noda, Chiba, Japan</subfield>
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   <subfield code="a">Yoshimoto</subfield>
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   <subfield code="u">Department of Industrial Chemistry, Tokyo University of Science, Noda, Chiba, Japan</subfield>
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   <subfield code="a">Aburai</subfield>
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   <subfield code="u">Department of Industrial Chemistry, Tokyo University of Science, Noda, Chiba, Japan</subfield>
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   <subfield code="a">Kanai</subfield>
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   <subfield code="u">Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda-shi, 278-8510, Chiba-Ken, Japan</subfield>
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   <subfield code="u">Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda-shi, 278-8510, Chiba-Ken, Japan</subfield>
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   <subfield code="u">Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda-shi, 278-8510, Chiba-Ken, Japan</subfield>
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   <subfield code="u">Department of Applied Biological Science, Faculty of Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda-shi, 278-8510, Chiba-Ken, Japan</subfield>
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   <subfield code="u">Department of Industrial Chemistry, Tokyo University of Science, Noda, Chiba, Japan</subfield>
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