Cloning, Sequencing, and Expression of a Thermostable Cellulase Gene ofHumicola grisea | Zendy

Shou Takashima | Zendy; Akira Nakamura | Zendy; Haruhiko Masaki | Zendy; Takeshi Uozumi | Zendy

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Cloning, Sequencing, and Expression of a Thermostable Cellulase Gene ofHumicola grisea

Author(s) -

Shou Takashima,

Akira Nakamura,

Haruhiko Masaki,

Takeshi Uozumi

Publication year - 1997

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.61.245

Subject(s) - cellulase , gene , biology , coding region , aspergillus oryzae , intron , microbiology and biotechnology , cloning (programming) , amino acid , tata box , peptide sequence , nucleic acid sequence , biochemistry , genetics , gene expression , enzyme , promoter , computer science , programming language

The egl2 gene coding a thermostable endoglucanase (EGL2) was cloned from Humicola grisea. The DNA sequence of egl2 predicted two putative introns in the coding region. The deduced amino acid sequence of EGL2 was 388 amino acids in length and showed 99.5% identity with the H. insolens CMC 3. In addition to TATA box and CAAT motifs, putative CREA binding sites were observed in the 5' upstream region of the egl2 gene. The egl2 gene was expressed in Aspergillus oryzae, and EGL2 was purified. EGL2 produced by A. oryzae showed a high activity toward carboxymethyl cellulose. The optimal temperature of EGL2 was 75 degrees C, and EGL2 had more than 80% residual activity after heating up to 75 degrees C for 10 min. This is the first report of enzymatic properties of the EGL2-type thermostable cellulase homologs from Humicola.

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