Enzymatic polymerization behavior using cellulose-binding domain deficient endoglucanase II.

Itsuko Nakamura; Hisanari Yoneda; Toshifumi Maeda; Akira Makino; Masashi Ohmae; Junji Sugiyama; Mitsuyoshi Ueda; Shiro Kobayashi; Shunsaku Kimura

doi:10.1002/mabi.200500044

PubMed · 15988789

Enzymatic polymerization behavior using cellulose-binding domain deficient endoglucanase II.

Itsuko Nakamura·Hisanari Yoneda·Toshifumi Maeda·Akira Makino·Masashi Ohmae·Junji Sugiyama·Mitsuyoshi Ueda·Shiro Kobayashi·Shunsaku Kimura

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Abstract

A mutant enzyme, EGII(core), in which the cellulose-binding domain was deleted from endoglucanase II from Trichoderma viride, was expressed in yeast, and the secreted enzyme was examined for the enzymatic polymerization to obtain artificial cellulose. EGII(core) polymerized beta-cellobiosyl fluoride to afford crystalline cellulose of type II. Comparison of the polymerization behavior of EGII(core) with that of EGII revealed the following: i) the crystalline product obtained with EGII(core) was stable in the polymerization solution, although the product was readily hydrolyzed in the presence of EGII; ii) the turnover number of EGII(core) was as high as that of EGII; iii) EGII(core) produced highly crystalline cellulose. EGII(core) is therefore advantageous for enzymatic polymerization.

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Cellobiose Cellulase Cellulose Polymers Polysaccharides Protein Structure, Tertiary Saccharomyces cerevisiae Sequence Deletion Trichoderma Journal Article

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Itsuko Nakamura, Hisanari Yoneda, Toshifumi Maeda, Akira Makino, Masashi Ohmae, Junji Sugiyama, Mitsuyoshi Ueda, Shiro Kobayashi, Shunsaku Kimura. 2005-07-14. Enzymatic polymerization behavior using cellulose-binding domain deficient endoglucanase II.. https://doi.org/10.1002/mabi.200500044

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