Structure and characteristics of an endo-β-1,4-glucanase, isolated from Trametes hirsuta, with high degradation to crystalline cellulose

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  • NOZAKI Kouichi
    Department of Chemistry and Material Engineering, Faculty of Engineering, Shinshu University
  • SEKI Takahiro
    Department of Chemistry and Material Engineering, Faculty of Engineering, Shinshu University
  • MATSUI Keiko
    Department of Chemistry and Material Engineering, Faculty of Engineering, Shinshu University
  • MIZUNO Masahiro
    Department of Chemistry and Material Engineering, Faculty of Engineering, Shinshu University
  • KANDA Takahisa
    Department of Chemistry and Material Engineering, Faculty of Engineering, Shinshu University
  • AMANO Yoshihiko
    Department of Chemistry and Material Engineering, Faculty of Engineering, Shinshu University

書誌事項

タイトル別名
  • Structure and Characteristics of an Endo-.BETA.-1,4-glucanase, Isolated from Trametes hirsuta, with High Degradation to Crystalline Cellulose
  • Structure and characteristics of an endo v 1 4 glucanase isolated from Trametes hirsuta with high degradation to crystalline cellulose
  • Structure and Characteristics of an Endo-β-1,4-glucanase, Isolated from<i>Trametes hirsuta</i>, with High Degradation to Crystalline Cellulose

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抄録

Trametes hirsuta produced cellulose-degrading enzymes when it was grown in a cellulosic medium such as Avicel or wheat bran. An endo-β-1,4-glucanase (ThEG) was purified from the culture filtrate, and the gene and the cDNA were isolated. The gene consisted of an open reading frame encoding 384 amino acids, interrupted by 11 introns. The whole sequence showed high homology with that of family 5 glycoside hydrolase. The properties of the recombinant enzyme (rEG) in Aspergillus oryzae were compared with those of the En-1 from Irpex lacteus, which showed the highest homology among all the endoglucanases reported. The rEG activity against Avicel was about 8 times higher than that of En-1 when based on CMC degradation. A remarkable structural difference between the two enzymes was the length of the linker connecting the cellulose-binding domain to the catalytic domain.

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