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J Biol Chem, Vol. 275, Issue 3, 2009-2018, January 21, 2000

Biochemical Analysis of Recombinant Fungal Mutanases
A NEW FAMILY OF 1,3-GLUCANASES WITH NOVEL CARBOHYDRATE-BINDING DOMAINS^*

Claus C. Fuglsang^§, Randy M. Berka^¶, Jill A. Wahleithner^¶, Sakari Kauppinen, Jeffrey R. Shuster^¶, Grethe Rasmussen, Torben Halkier^**, Henrik Dalbøge, and Bernard Henrissat

From the  Novo Nordisk A/S, Bagsværd DK-2880, Denmark, ^¶ Novo Nordisk Biotech, Inc., Davis, California 95616, and  Architecture et Fonction des Macromolécules Biologiques, CNRS-IFR1, 13402 Marseille, France

Nucleotide sequence analysis shows that Trichoderma harzianum and Penicillium purpurogenum 1,3-glucanases (mutanases) have homologous primary structures (53% amino acid sequence identity), and are composed of two distinct domains: a NH₂-terminal catalytic domain and a putative COOH-terminal polysaccharide-binding domain separated by a O-glycosylated Pro-Ser-Thr-rich linker peptide. Each mutanase was expressed in Aspergillus oryzae host under the transcriptional control of a strong -amylase gene promoter. The purified recombinant mutanases show a pH optimum in the range from pH 3.5 to 4.5 and a temperature optimum around 50-55 °C at pH 5.5. Also, they exhibit strong binding to insoluble mutan with K_D around 0.11 and 0.13 µM at pH 7 for the P. purpurogenum and T. harzianum mutanases, respectively. Partial hydrolysis showed that the COOH-terminal domain of the T. harzianum mutanase binds to mutan. The catalytic domains and the binding domains were assigned to a new family of glycoside hydrolases and to a new family of carbohydrate-binding domains, respectively.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EMBL Data Bank with accession number(s) AF214480 (T. harzianum mutanase gene sequence previously listed as Geneseq^TM accession number V12368) and AF214481 (P. purpurogenum mutanase gene sequence; previously listed as Geneseq^TM accession number V81911).

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