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Molecular characterization and heterologous expression of the gene encoding a low-molecular-mass endoglucanase from Trichoderma reesei QM9414

Article Abstract:

Genomic and cDNA clones encoding EG III were isolated to characterize and determine the heterologous expression of the gene encoding a low-molecular-mass endoglucanase from Trichoderma reesei QM9414. The nucleotide sequence of the cDNA fragment was verified to contain a 702-bp open reading frame that encodes a 234-amino-acid propeptide. The protein sequence was found to contain significant homologies with family H endo-beta-1,4-glucanases. The 16-amino-acid N-terminal sequence was shown to function as a leader peptide for possible secretion.

Author: Okada, Hirofumi, Morikawa, Yasushi, Tada, Kohji, Sekiya, Tadashi, Yokoyama, Kengo, Takahashi, Akinori, Tohda, Hideki, Kumagai, Hiromichi
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
Cloning, Circular DNA, Cellulose, Amino acid sequence, Amino acid sequencing

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An alpha-L-arabinofuranosidase from Trichoderma reesei containing a noncatalytic xylan-binding domain

Article Abstract:

Research was conducted to examine an alpha-L-arabinofuranosidase (alpha-AF) from Trichoderma reesei containing a noncatalytic xylan-binding domain. The alpha-AF was purified and partially characterized and its cDNA was cloned. It was observed in the preliminary results that alpha-AF activity was induced by L-sorbose, an excellent inducer for the production of xylanase and cellulase by T reesei. It is concluded that the enzyme having the lower molecular mass is the truncated form of the enzyme with the higher molecular mass.

Author: Nogawa, Masahiro, Okada, Hirofumi, Morikawa, Yasushi, Yatsui, Kenji, Tomioka, Akiko
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1999
Microbial enzymes, Enzyme kinetics

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Purification and characterization of exo-beta-D-glucosaminidase from a cellulolytic fungus, Trichoderma reesei PC-3-7

Article Abstract:

Tbe identification, purification and characterization of the exo-beta-D-glucosaminidase from the hyper-cellulolytic fungus, Trichoderma cellulolytic fungus, Trichoderma reesei PC-3-7, are described. The exo-beta-D-glucosaminidase was found to possess a retaining catalytic mechanism as it produced a beta-form of glucosamine (GlcN) and to continuously release one GlcN residue from the nonreducing end of the substrate.

Author: Nogawa, Masahiro, Takahashi, Hiroya, Kashiwagi, Aya, Ohshima, Kenji, Okada, Hirofumi, Morikawa, Yasushi
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
Genetic aspects, Enzymes, Fungi, Enzyme structure-activity relationships, Glucose

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Subjects list: Research
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